Academic literature on the topic 'SUMO Protease'
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Journal articles on the topic "SUMO Protease"
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Yang, Wei, Liangli Wang, and Wulf Paschen. "Development of a High-Throughput Screening Assay for Inhibitors of Small Ubiquitin-Like Modifier Proteases." Journal of Biomolecular Screening 18, no. 5 (March 7, 2013): 621–28. http://dx.doi.org/10.1177/1087057113479971.
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Small ubiquitin-like modifier (SUMO1–3) is a small group of proteins that are ligated to lysine residues in target proteins. SUMO conjugation is a highly dynamic process, as SUMOylated proteins are rapidly deconjugated by SUMO proteases. SUMO conjugation/deconjugation plays pivotal roles in major cellular pathways and is associated with a number of pathological conditions. It is therefore of significant clinical interest to develop new strategies to screen for compounds to specifically interfere with SUMO conjugation/deconjugation. Here, we describe a novel high-throughput screening (HTS)–compatible assay to identify inhibitors of SUMO proteases. The assay is based on AlphaScreen technology and uses His-tagged SUMO2 conjugated to Strep-tagged SUMO3 as a SUMO protease substrate. A bacterial SUMOylation system was used to generate this substrate. A three-step purification strategy was employed to yield substrate of high quality. Our data indicated that this unique substrate can be readily detected in the AlphaScreen assays in a dose-dependent manner. Cleavage reactions by SUMO protease with or without inhibitor were monitored based on AlphaScreen signals. Furthermore, the assay was adapted to a 384-well format, and the interplate and interday variability was evaluated in eight 384-well plates. The average Z′ factor was 0.83 ± 0.04, confirming the suitability for HTS applications.
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Mukhopadhyay, Debaditya, Ferhan Ayaydin, Nagamalleswari Kolli, Shyh-Han Tan, Tadashi Anan, Ai Kametaka, Yoshiaki Azuma, Keith D. Wilkinson, and Mary Dasso. "SUSP1 antagonizes formation of highly SUMO2/3-conjugated species." Journal of Cell Biology 174, no. 7 (September 21, 2006): 939–49. http://dx.doi.org/10.1083/jcb.200510103.
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Small ubiquitin-related modifier (SUMO) processing and deconjugation are mediated by sentrin-specific proteases/ubiquitin-like proteases (SENP/Ulps). We show that SUMO-specific protease 1 (SUSP1), a mammalian SENP/Ulp, localizes within the nucleoplasm. SUSP1 depletion within cell lines expressing enhanced green fluorescent protein (EGFP) fusions to individual SUMO paralogues caused redistribution of EGFP-SUMO2 and -SUMO3, particularly into promyelocytic leukemia (PML) bodies. Further analysis suggested that this change resulted primarily from a deficit of SUMO2/3-deconjugation activity. Under these circumstances, PML bodies became enlarged and increased in number. We did not observe a comparable redistribution of EGFP-SUMO1. We have investigated the specificity of SUSP1 using vinyl sulfone inhibitors and model substrates. We found that SUSP1 has a strong paralogue bias toward SUMO2/3 and that it acts preferentially on substrates containing three or more SUMO2/3 moieties. Together, our findings argue that SUSP1 may play a specialized role in dismantling highly conjugated SUMO2 and -3 species that is critical for PML body maintenance.
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Alegre, Kamela O., and David Reverter. "Swapping Small Ubiquitin-like Modifier (SUMO) Isoform Specificity of SUMO Proteases SENP6 and SENP7." Journal of Biological Chemistry 286, no. 41 (August 30, 2011): 36142–51. http://dx.doi.org/10.1074/jbc.m111.268847.
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SUMO proteases can regulate the amounts of SUMO-conjugated proteins in the cell by cleaving off the isopeptidic bond between SUMO and the target protein. Of the six members that constitute the human SENP/ULP protease family, SENP6 and SENP7 are the most divergent members in their conserved catalytic domain. The SENP6 and SENP7 subclass displays a clear proteolytic cleavage preference for SUMO2/3 isoforms. To investigate the structural determinants for such isoform specificity, we have identified a unique sequence insertion in the SENP6 and SENP7 subclass that is essential for their proteolytic activity and that forms a more extensive interface with SUMO during the proteolytic reaction. Furthermore, we have identified a region in the SUMO surface determinant for the SUMO2/3 isoform specificity of SENP6 and SENP7. Double point amino acid mutagenesis on the SUMO surface allows us to swap the specificity of SENP6 and SENP7 between the two SUMO isoforms. Structure-based comparisons combined with biochemical and mutagenesis analysis have revealed Loop 1 insertion in SENP6 and SENP7 as a platform to discriminate between SUMO1 and SUMO2/3 isoforms in this subclass of the SUMO protease family.
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Liu, Yan, Yali Shen, Yang Song, Lei Xu, J. Jefferson P. P. Perry, and Jiayu Liao. "Isopeptidase Kinetics Determination by a Real Time and Sensitive qFRET Approach." Biomolecules 11, no. 5 (April 30, 2021): 673. http://dx.doi.org/10.3390/biom11050673.
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Isopeptidase activity of proteases plays critical roles in physiological and pathological processes in living organisms, such as protein stability in cancers and protein activity in infectious diseases. However, the kinetics of protease isopeptidase activity has not been explored before due to a lack of methodology. Here, we report the development of novel qFRET-based protease assay for characterizing the isopeptidase kinetics of SENP1. The reversible process of SUMOylation in vivo requires an enzymatic cascade that includes E1, E2, and E3 enzymes and Sentrin/SUMO-specific proteases (SENPs), which can act either as endopeptidases that process the pre-SUMO before its conjugation, or as isopeptidases to deconjugate SUMO from its target substrate. We first produced the isopeptidase substrate of CyPet-SUMO1/YPet-RanGAP1c by SUMOylation reaction in the presence of SUMO E1 and E2 enzymes. Then a qFRET analyses of real-time FRET signal reduction of the conjugated substrate of CyPet-SUMO1/YPet-RanGAP1c to free CyPet-SUMO1 and YPet-RanGAP1c by the SENP1 were able to obtain the kinetic parameters, Kcat, KM, and catalytic efficiency (Kcat/KM) of SENP1. This represents a pioneer effort in isopeptidase kinetics determination. Importantly, the general methodology of qFRET-based protease isopeptidase kinetic determination can also be applied to other proteases.
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Lee, Jiwon, Yool Lee, Min Joo Lee, Eonyoung Park, Sung Hwan Kang, Chin Ha Chung, Kun Ho Lee, and Kyungjin Kim. "Dual Modification of BMAL1 by SUMO2/3 and Ubiquitin Promotes Circadian Activation of the CLOCK/BMAL1 Complex." Molecular and Cellular Biology 28, no. 19 (July 21, 2008): 6056–65. http://dx.doi.org/10.1128/mcb.00583-08.
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ABSTRACT Heterodimers of BMAL1 and CLOCK drive rhythmic expression of clock-controlled genes, thereby generating circadian physiology and behavior. Posttranslational modifications of BMAL1 play a key role in modulating the transcriptional activity of the CLOCK/BMAL1 complex during the circadian cycle. Recently, we demonstrated that circadian activation of the heterodimeric transcription factor is accompanied by ubiquitin-dependent proteolysis of BMAL1. Here we show that modification by SUMO localizes BMAL1 exclusively to the promyelocytic leukemia nuclear body (NB) and simultaneously promotes its transactivation and ubiquitin-dependent degradation. Under physiological conditions, BMAL1 was predominantly conjugated to poly-SUMO2/3 rather than SUMO1, and the level of these conjugates underwent rhythmic variation, peaking at times of maximum E-box-mediated circadian transcription. Interestingly, mutation of the sumoylation site (Lys259) of BMAL1 markedly inhibited both its ubiquitination and its proteasome-mediated proteolysis, and these effects were reversed by covalent attachment of SUMO3 to the C terminus of the mutant BMAL1. Consistent with this, SUSP1, a SUMO protease highly specific for SUMO2/3, abolished ubiquitination, as well as sumoylation of BMAL1, while the ubiquitin protease UBP41 blocked BMAL1 ubiquitination but induced accumulation of polysumoylated BMAL1 and its localization to the NB. Furthermore, inhibition of proteasome with MG132 elicited robust nuclear accumulation of SUMO2/3- and ubiquitin-modified BMAL1 that was restricted to the transcriptionally active stage of the circadian cycle. These results indicate that dual modification of BMAL1 by SUMO2/3 and ubiquitin is essential for circadian activation and degradation of the CLOCK/BMAL1 complex.
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Shen, Lin Nan, Changjiang Dong, Huanting Liu, James H. Naismith, and Ronald T. Hay. "The structure of SENP1–SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing." Biochemical Journal 397, no. 2 (June 28, 2006): 279–88. http://dx.doi.org/10.1042/bj20052030.
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The SUMO (small ubiquitin-like modifier)-specific protease SENP1 (sentrin-specific protease 1) can process the three forms of SUMO to their mature forms and deconjugate SUMO from modified substrates. It has been demonstrated previously that SENP1 processed SUMO-1 more efficiently than SUMO-2, but displayed little difference in its ability to deconjugate the different SUMO paralogues from modified substrates. To determine the basis for this substrate specificity, we have determined the crystal structure of SENP1 in isolation and in a transition-state complex with SUMO-2. The interface between SUMO-2 and SENP1 has a relatively poor complementarity, and most of the recognition is determined by interaction between the conserved C-terminus of SUMO-2 and the cleft in the protease. Although SENP1 is rather similar in structure to the related protease SENP2, these proteases have different SUMO-processing activities. Electrostatic analysis of SENP1 in the region where the C-terminal peptide, removed during maturation, would project indicates that it is the electrostatic complementarity between this region of SENP1 and the C-terminal peptides of the various SUMO paralogues that mediates selectivity.
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Vertegaal, Alfred C. O. "SUMO chains: polymeric signals." Biochemical Society Transactions 38, no. 1 (January 19, 2010): 46–49. http://dx.doi.org/10.1042/bst0380046.
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Ubiquitin and ubiquitin-like proteins are conjugated to a wide variety of target proteins that play roles in all biological processes. Target proteins are conjugated to ubiquitin monomers or to ubiquitin polymers that form via all seven internal lysine residues of ubiquitin. The fate of these target proteins is controlled in a chain architecture-dependent manner. SUMO (small ubiquitin-related modifier) shares the ability of ubiquitin to form chains via internal SUMOylation sites. Interestingly, a SUMO-binding site in Ubc9 is important for SUMO chain synthesis. Similar to ubiquitin–polymer cleavage by USPs (ubiquitin-specific proteases), SUMO chain formation is reversible. SUMO polymers are cleaved by the SUMO proteases SENP6 [SUMO/sentrin/SMT3 (suppressor of mif two 3)-specific peptidase 6], SENP7 and Ulp2 (ubiquitin-like protease 2). SUMO chain-binding proteins including ZIP1, SLX5/8 (synthetic lethal of unknown function 5/8), RNF4 (RING finger protein 4) and CENP-E (centromere-associated protein E) have been identified that interact non-covalently with SUMO chains, thereby regulating target proteins that are conjugated to SUMO multimers. SUMO chains play roles in replication, in the turnover of SUMO targets by the proteasome and during mitosis and meiosis. Thus signalling via polymers is an exciting feature of the SUMO family.
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Xu, Zheng, So Fun Chau, Kwok Ho Lam, Ho Yin Chan, Tzi Bun Ng, and Shannon W. N. Au. "Crystal structure of the SENP1 mutant C603S–SUMO complex reveals the hydrolytic mechanism of SUMO-specific protease." Biochemical Journal 398, no. 3 (August 29, 2006): 345–52. http://dx.doi.org/10.1042/bj20060526.
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SUMO (small ubiquitin-related modifier)-specific proteases catalyse the maturation and de-conjugation processes of the sumoylation pathway and modulate various cellular responses including nuclear metabolism and cell cycle progression. The active-site cysteine residue is conserved among all known SUMO-specific proteases and is not substitutable by serine in the hydrolysis reactions demonstrated previously in yeast. We report here that the catalytic domain of human protease SENP1 (SUMO-specific protease 1) mutant SENP1CC603S carrying a mutation of cysteine to serine at the active site is inactive in maturation and de-conjugation reactions. To further understand the hydrolytic mechanism catalysed by SENP1, we have determined, at 2.8 Å resolution (1 Å=0.1 nm), the X-ray structure of SENP1CC603S–SUMO-1 complex. A comparison of the structure of SENP2–SUMO-1 suggests strongly that SUMO-specific proteases require a self-conformational change prior to cleavage of peptide or isopeptide bond in the maturation and de-conjugation processes respectively. Moreover, analysis of the interface of SENP1 and SUMO-1 has led to the identification of four unique amino acids in SENP1 that facilitate the binding of SUMO-1. By means of an in vitro assay, we further demonstrate a novel function of SENP1 in hydrolysing the thioester linkage in E1-SUMO and E2-SUMO complexes. The results disclose a new mechanism of regulation of the sumoylation pathway by the SUMO-specific proteases.
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Di Bacco, Alessandra, Jian Ouyang, Hsiang-Ying Lee, Andre Catic, Hidde Ploegh, and Grace Gill. "The SUMO-Specific Protease SENP5 Is Required for Cell Division." Molecular and Cellular Biology 26, no. 12 (June 15, 2006): 4489–98. http://dx.doi.org/10.1128/mcb.02301-05.
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ABSTRACT Posttranslational modification of substrates by the small ubiquitin-like modifier, SUMO, regulates diverse biological processes, including transcription, DNA repair, nucleocytoplasmic trafficking, and chromosome segregation. SUMOylation is reversible, and several mammalian homologs of the yeast SUMO-specific protease Ulp1, termed SENPs, have been identified. We demonstrate here that SENP5, a previously uncharacterized Ulp1 homolog, has SUMO C-terminal hydrolase and SUMO isopeptidase activities. In contrast to other SENPs, the C-terminal catalytic domain of SENP5 preferentially processed SUMO-3 compared to SUMO-1 precursors and preferentially removed SUMO-2 and SUMO-3 from SUMO-modified RanGAP1 in vitro. In cotransfection assays, SENP5 preferentially reduced high-molecular-weight conjugates of SUMO-2 compared to SUMO-1 in vivo. Full-length SENP5 localized to the nucleolus. Deletion of the noncatalytic N-terminal domain led to loss of nucleolar localization and increased de-SUMOylation activity in vivo. Knockdown of SENP5 by RNA interference resulted in increased levels of SUMO-1 and SUMO-2/3 conjugates, inhibition of cell proliferation, defects in nuclear morphology, and appearance of binucleate cells, revealing an essential role for SENP5 in mitosis and/or cytokinesis. These findings establish SENP5 as a SUMO-specific protease required for cell division and suggest that mechanisms involving both the catalytic and noncatalytic domains determine the distinct substrate specificities of the mammalian SUMO-specific proteases.
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Dorval, Véronique, Matthew J. Mazzella, Paul M. Mathews, Ronald T. Hay, and Paul E. Fraser. "Modulation of Aβ generation by small ubiquitin-like modifiers does not require conjugation to target proteins." Biochemical Journal 404, no. 2 (May 14, 2007): 309–16. http://dx.doi.org/10.1042/bj20061451.
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The sequential processing of the APP (amyloid precursor protein) by the β- and γ-secretase and generation of the Aβ (amyloid-β) peptide is a primary pathological factor in AD (Alzheimer's disease). Regulation of the processing or turnover of these proteins represents potential targets for the development of AD therapies. Sumoylation is a process by which SUMOs (small ubiquitin-like modifiers) are covalently conjugated to target proteins, resulting in a number of functional consequences. These include regulation of protein–protein interactions, intracellular trafficking and protein stability, which all have the potential to impact on several aspects of the amyloidogenic pathway. The present study examines the effects of overexpression and knockdown of the major SUMO isoforms (SUMO1, 2 and 3) on APP processing and the production of Aβ peptides. SUMO3 overexpression significantly increased Aβ40 and Aβ42 secretion, which was accompanied by an increase in full-length APP and its C-terminal fragments. These effects of SUMO3 were independent of its covalent attachment or chain formation, as mutants lacking the motifs responsible for SUMO chain formation or SUMO conjugation led to similar changes in Aβ. SUMO3 overexpression also up-regulated the expression of the transmembrane protease BACE (β-amyloid-cleaving enzyme), but failed to affect levels of several other unrelated proteins. Suppression of SUMO1 or combined SUMO2+3 by RNA interference did not affect APP levels or Aβ production. These findings confirm a specific effect of SUMO3 overexpression on APP processing and the production of Aβ peptides but also suggest that endogenous sumoylation is not essential and likely plays an indirect role in modulating the amyloid processing pathway.
Dissertations / Theses on the topic "SUMO Protease"
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Elmore, Zachary Cole. "SUMO-Dependent Substrate Targeting of the SUMO Protease Ulp1." W&M ScholarWorks, 2011. https://scholarworks.wm.edu/etd/1539626905.
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Hattersley, Neil. "Characterisation of the SUMO protease SenP6." Thesis, University of Dundee, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.521677.
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Guillotte, Mark. "Identifying SUMO Protease Targets and Investigating E3 Ligase Interactions." W&M ScholarWorks, 2014. https://scholarworks.wm.edu/etd/1539626956.
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CASTELLUCCI, FEDERICA. "THE ROLE OF THE S. CEREVISIAE SUMO PROTEASE ULP2 IN DNA REPLICATION AND GENOME INTEGRITY." Doctoral thesis, Università degli Studi di Milano, 2011. http://hdl.handle.net/2434/155578.
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Sumoylation has emerged as an important player in several biological processes involved in the maintenance of genome stability. A number of proteins implicated in DNA metabolism-associated processes, such as DNA replication, repair and chromosome segregation, were shown to sumoylated. Moreover, alterations in protein sumoylation and desumoylation, caused by deregulation of enzymes involved in the SUMO pathway, were associated with cancer development. Work done previously in our laboratory and by other groups suggested an important role for sumoylation in promoting DNA damage tolerance. However, the molecular mechanisms by which DNA damage regulates sumoylation and how balance between sumoylation and desumoylation impinges the cellular response to genotoxic stress are questions that need to be clarified.
Different scenarios could account for regulating sumoylation, one of which envisages a control over the activity of the desumoylating enzymes. Budding yeast has two desumoylating enzymes, Ulp1 and Ulp2, which have distinct cellular localization and enzymatic activities. Starting by investigating whether Ulp1 and/or Ulp2 undergo any type of functional regulation, I found the nuclear SUMO protease Ulp2 to be phosphorylated both in a cell cycle-dependent manner and in response to replication stress or DNA damage.
The present work aimed at studying the molecular mechanisms through which Ulp2 promotes genome integrity, both in physiological conditions and in conditions of replication stress. By examining the genome-wide localization of Ulp2 by ChIP-on-chip I observed that Ulp2 is bound to centromeric regions throughout the cell cycle and this enrichment is extended to pericentromeric regions in cells arrested at metaphase. Lack of Ulp2 affects the chromatin structure at centromeres and nearby regions. Following replication stress, Ulp2 is bound to most of the origins of replication that are active under our experimental conditions and is required for efficient origin firing. Also under conditions of replication stress Ulp2 is important for the maintenance of chromatin structure and for the binding of histone variants that are known to play a role in damage tolerance to origins of replication. Thus, Ulp2 appears to play key roles in regulating the status of chromatin to make it suitable for efficient replication and chromosome segregation.
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Era, Saho. "The SUMO protease SENP1 is required for cohesion maintenance and mitotic arrest following spindle poison treatment." Kyoto University, 2013. http://hdl.handle.net/2433/174794.
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Eckhoff, Julia [Verfasser], Jürgen [Gutachter] Dohmen, and Kay [Gutachter] Hofmann. "Mechanistic and structural characterization of the SUMO-specific protease Ulp2 / Julia Eckhoff ; Gutachter: Jürgen Dohmen, Kay Hofmann." Köln : Universitäts- und Stadtbibliothek Köln, 2016. http://d-nb.info/1115330659/34.
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Maroui, Mohamed Ali. "Rôle et devenir de PML lors de l’infection par l’EMCV." Thesis, Paris 11, 2012. http://www.theses.fr/2012PA11T008/document.
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PML et les corps nucléaires (CN) sont impliqués dans la défense antivirale. En effet, notre équipe a montré que la surexpression de PMLIII confère la résistance au virus de la stomatite vésiculaire, au virus de l'influenza, au virus foamy mais pas au virus de l’encéphalomyocardite (EMCV). J’ai montré dans mon travail de thèse que l’EMCV contrecarre le pouvoir antiviral de PMLIII en induisant sa dégradation par un processus dépendant du protéasome et de SUMO. Cependant, les cellules de souris invalidées pour PML sont plus sensibles à l’infection par l’EMCV que les cellules issues de souris parentales. Pour déterminer l’isoforme de PML responsable de cet effet antiviral, j’ai analysé l’effet des sept isoformes de PML (PMLI-VII) et j’ai montré que seule l’expression en stable de PMLIV confère la résistance à l’EMCV en séquestrant la polymérase virale 3Dpol au sein des CN PML. De plus la déplétion de PMLIV augmente la production de l’EMCV dans les cellules traitées par l’interféron. Ces données indiquent le mécanisme par lequel PML confère la résistance à l’EMCV et révèlent que PML est l’une des protéines médiatrices des effets anti-EMCV de l’interféronPML and nuclear bodies (NBs) are implicated in antiviral defense. Indeed, our team showed that overexpression of PMLIII confers resistance to vesicular stomatitis virus, influenza virus, foamy virus but not to encephalomyocarditis virus (EMCV). I have shown during my thesis that EMCV counteracts the antiviral effect of PMLIII by inducing its degradation in SUMO and proteasome-dependent way. However, cells derived from PML knockout mice are more susceptible to EMCV infection than wild-type cells. To determine the isoforme of PML implicated in this antiviral effect, I analysed the effect of the seven PML isoforms (PMLI-PMLVII) and I showed that only stable expression of PMLIV confers resistance to EMCV by sequestring the viral polymérase 3Dpol in PML Nbs. In addition, depletion of PMLIV boosted EMCV production in interferon-treated cells. These finding sindicate the mechanism by which PML confers resistance to EMCV and reveal a new pathway mediating the antiviral activity of interferon against EMCV
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Rouvière, Jérôme. "Etude du rôle de la sumoylation dans le métabolisme des ribonucléoparticules d'ARN messagers (mRNPs)." Thesis, Université Paris-Saclay (ComUE), 2016. http://www.theses.fr/2016SACLS069.
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Au sein des cellules, les ARNms sont liés par de nombreuses protéines, générant ainsi des particules appelées mRNPs (Ribonucléoparticules de messagers). Leur formation est cotranscriptionnelle, et leur composition va réguler l’ensemble des étapes du métabolisme des ARNms : stabilité, maturation, export, localisation et traduction. Au vu de l’importance de ces mécanismes dans la physiologie cellulaire, le contenu protéique des mRNPs est finement régulé dans le temps et l’espace et fait l’objet de nombreux remodelages. Ces changements de composition dépendent notamment des hélicases, ainsi que des modifications post-traductionnelles ; cependant, ces mécanismes demeurent à caractériser de façon plus approfondie. Une modification post-traductionnelle susceptible de moduler ces remaniements depuis la levure S. cerevisiae jusqu’aux métazoaires est la sumoylation. En effet, la SUMO-protéase Ulp1/SENP2, une enzyme clé de la machinerie de sumoylation, est localisée au panier des pores nucléaires, à proximité d’une plateforme d’ancrage des mRNPs destinées à l’export. Par ailleurs, il a été rapporté chez la levure que des mutants affectant la localisation et la stabilité d’Ulp1 présentent des défauts d’export et de localisation des mRNPs. Au vu de ces données, le laboratoire s’est intéressé aux rôles potentiels de la sumoylation dans le métabolisme de ces particules d’ARNm. Dans ce but, un crible protéomique a été réalisé chez la levure S. cerevisiae afin de comparer la composition des mRNPs entre des cellules sauvages ou mutantes pour Ulp1. Ce crible a mis en évidence un rôle d’Ulp1 dans le recrutement de deux composants des mRNPs, le complexe THO et l’hnRNP Hek2. Le complexe THO est un facteur multiprotéique qui participe à la prévention de l’instabilité génique et contribue à la transcription des ARNms, à l’assemblage des mRNPs et à leur export. L’hnRNP Hek2 est une protéine aux rôles multiples, dont l’association à un ARNm est susceptible de moduler sa stabilité, sa traduction et/ou sa localisation. Des analyses biochimiques nous ont permis de mettre en évidence l’existence de formes sumoylées de la sous-unité Hpr1 du complexe THO ainsi que de l’hnRNP Hek2. Toutes deux sont Ulp1-dépendantes, et interviennent sur la partie C-terminale de ces protéines. Nous avons également mis en évidence que chacune de ces sumoylations contrôle le recrutement de son substrat au sein des mRNPs. L’analyse fonctionnelle d’un mutant affectant la sumoylation d’Hpr1 a identifié cette modification comme nécessaire au recrutement du complexe THO sur une population d’ARNms impliqués dans la résistance au stress acide, autrement dégradés par l’exosome. Ainsi, l’absence de sumoylation d’Hpr1 diminue fortement la viabilité cellulaire en conditions de stress, un phénotype supprimé par l’inactivation de l’exosome. L’étude des effets de la sumoylation d’Hek2 suggère une modulation par SUMO de certaines de ses fonctions, notamment dans la localisation cellulaire des ARNms. L’ensemble de ces données fournit donc les deux premiers exemples de régulation du métabolisme des mRNPs par des événements de sumoylation intervenant au niveau du pore nucléaireWithin the cells, mRNAs are associated to proteins, thereby generating particles called mRNPs (messenger ribonucleoproteins). mRNPs form in a cotranscriptional manner and their composition defines the fate of mRNAs by modulating the different steps of their metabolism, including their stability, their processing, their export, their localisation and their translation. In view of the importance of such mechanisms for cell physiology, several mechanisms ensure a tight spatio-temporal control of mRNPs composition through multiple mRNP remodelling events. These changes in the protein content of mRNPs depend on helicases and post-translational modifications, but remain to be further investigated. Sumoylation is one of the modifications that could contribute to mRNPs remodelling from yeast (S. cerevisiae) to metazoans. Indeed, it has been reported that the SUMO-protease Ulp1/SENP2, a key enzyme of the sumoylation machinery, is localized at the basket of nuclear pore complexes, in close vicinity with mRNPs committed for export. This particular localization, together with the reported defects in mRNPs export and localisation of yeast mutants affecting Ulp1, prompted the lab to ask whether sumoylation could contribute to mRNP biogenesis. In order to investigate this hypothesis, our lab compared mRNPs composition between wild-type and ulp1 mutant S. cerevisiae yeast strains using a proteomic approach. This screen identified two mRNP components that depend on Ulp1 for their recruitment onto these particles: the THO complex and the hnRNP Hek2. The THO complex is a multi-subunit factor that prevents genome instability and contributes to transcription, mRNP assembly and export. Hek2 has multiple functions in mRNA stability, translation and/or localization. Using biochemical approaches, we have been able to visualize sumoylated versions of the Hpr1 subunit of the THO complex and of the hnRNP Hek2. In both cases, this modification depends on Ulp1 activity and occurs on the C-terminal part of the protein. We further showed that these sumoylation events control THO and Hek2 recruitment onto mRNPs. Functional analysis of a mutant impairing Hpr1 sumoylation revealed that this modification is required for proper recruitment of the THO complex onto a subset of mRNAs involved in acidic stress resistance, which are otherwise degraded by the exosome. Decreased Hpr1 sumoylation results in a strong reduction of viability in acid stress conditions, a phenotype that is rescued by inactivation of the exosome. The investigation of the role of Hek2 sumoylation in mRNPs metabolism suggests that this modification regulates some of Hek2 functions, especially in mRNA localisation. All together, these results provide the two first examples of mRNPs components whose functions are regulated by sumoylation events occurring at the level of nuclear pores
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Ulbricht, David, Jan Pippel, Stephan Schultz, René Meier, Norbert Sträter, and John T. Heiker. "A unique serpin P1′ glutamate and a conserved β-sheet C arginine are key residues for activity, protease recognition and stability of serpinA12 (vaspin)." Portland Press, 2015. https://ul.qucosa.de/id/qucosa%3A33439.
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SerpinA12 (vaspin) is thought to be mainly expressed in adipose tissue and has multiple beneficial effects on metabolic, inflammatory and atherogenic processes related to obesity. KLK7 (kallikrein 7) is the only known protease target of vaspin to date and is inhibited with a moderate inhibition rate. In the crystal structure, the cleavage site (P1-P1′) of the vaspin reactive centre loop is fairly rigid compared with the flexible residues before P2, possibly supported by an ionic interaction of P1′ glutamate (Glu379) with an arginine residue (Arg302) of the β-sheet C. A P1′ glutamate seems highly unusual and unfavourable for the protease KLK7. We characterized vaspin mutants to investigate the roles of these two residues in protease inhibition and recognition by vaspin. Reactive centre loop mutations changing the P1′ residue or altering the reactive centre loop conformation significantly increased inhibition parameters, whereas removal of the positive charge within β-sheet C impeded the serpin–protease interaction. Arg302 is a crucial contact to enable vaspin recognition by KLK7 and it supports moderate inhibition of the serpin despite the presence of the detrimental P1′ Glu379, which clearly represents a major limiting factor for vaspin-inhibitory activity. We also show that the vaspin-inhibition rate for KLK7 can be modestly increased by heparin and demonstrate that vaspin is a heparin-binding serpin. Noteworthily, we observed vaspin as a remarkably thermostable serpin and found that Glu379 and Arg302 influence heat-induced polymerization. These structural and functional results reveal the mechanistic basis of how reactive centre loop sequence and exosite interaction in vaspin enable KLK7 recognition and regulate protease inhibition as well as stability of this adipose tissue-derived serpin.
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Alegre, Kamela Olivya. "Structural and Fumctional Analysis of the SUMO Proteases SENP6 and SENP7." Doctoral thesis, Universitat Autònoma de Barcelona, 2012. http://hdl.handle.net/10803/121596.
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Intercambiar la especifidad de las isoformas de SUMO1 y SUMO2/3 para SENP6/SENP7
SENP6 y SENP7 son los miembros más divergentes de la familia de proteasas SENP y los únicos miembros que llevan cuatro inserciónes o “loops” localizadas en su dominio catalítico. Al sobreponer el dominio catalítico de SENP7 sobre el complejo SENP2-SUMO podemos ver una posible interfaz entre el Loop1 de SENP7 y SUMO. También identificamos diferentes residuos de SUMO1 y SUMO2 que podrían formar parte de la interfaz. Diseñamos una serie de mutantes de SUMO1 y SUMO2 donde se intercambian entre ellos los residuos que forman parte de la interfaz. De esta manera fuimos capaces de intercambiar la actividad proteolítica de SENP6 y SENP7 hacia estos substratos.
El Loop1 de SENP6 y SENP7 es responsable de la especificidad de la interfaz entre los SUMOs y las SENP6/7
Diseñamos una serie de mutantes del Loop1 de SENP7 dentro de la posible interfaz entre el Loop1 de SENP7 y SUMO para determinar los papeles estructurales y funcionales de los residuos que están dentro de esta región. Los mutantes de SENP6/7 sin el Loop1 perdían gran parte de su actividad, esta se podía recuperar un poco al reemplazar las cuatro prolinas del Loop1 por glicinas. De esta manera probamos que el Loop1 tiene un papel por lo menos estructural en el reconocimiento de SUMO. También identificamos el residuo Lys691 del Loop1 de SENP7 como elemento indispensable en la actividad de la enzima ya que al mutar este residuo por un aspártico disminuye la actividad para sustratos con SUMO2. Por otra parte el residuo Asp71 de SUMO2 es uno de los residuos propuestos para el reconocimiento de SUMO2/3. Cuando mutamos este residuo a lisina, vemos una bajada en la actividad de SENP7. Este hecho sugiere que Asp71 de SUMO2 está interaccionando con Loop1 y quizas con la Lys691, y que la bajada en la actividad es causada por una repulsión de cargas.
Por otro lado con el objectivo de estudiar el efecto de Loop1 en la desconjugación de especies SUMOyladas, insertamos los ocho residuos de SENP6 Loop en el dominio catalítico de SENP2. Esta inserción provoca un aumento de la actividad sustancial de SENP2 contra diSUMO en comparación con la forma wild type.
Complejos con substratos
Para ver si SENP6 es capaz de formar algún complejo estable, producimos cantidades en miligramos de los mutantes inactivos de Δ3SENP6C1030S y de Δ2Δ3SENP6C1030S. Incubamos cada proteasa con los precursors de SUMO, con RanGAP1-SUMO2 y con diSUMO2. De todos los substratos que probamos, diSUMO2 fue el único que podía formar un complejo estable con Δ3SENP6CS y Δ2Δ3SENP6CS por copurificación en una columna de gel fitración. Con Δ2SENP6CS no pudimos formar ningún complejo. Con esta información llegamos a la conclusión que el Loop3 de SENP6 reduce, quizá por razones de entropía, la capacidad de SENP6 de formar un complejo estable con diSUMO2.
Caracterización del Loop3 de SENP6
Para descifrar el papel que este loop tiene en el contexto de la proteasa, producimos y purificamos los 185 residuos de Loop3 de SENP6. Análysis 1-H 1-D RMN mostraba una falta de estructura terciaria dentro del loop, pero proteólisis limitada y espectroscopia de masas mostraban un fragmento estable de cerca de 11kDa. Dicroísmo circular y FTIR tambien sugieren la presencia de algunos elementos de estructura secundaria. Globalmente, la caracterización biofísica del Loop3 de SENP6 muestra que el loop es una proteína desestructurada.Swapping the SUMO Isoform Specificity of SENP6/7 SENP6 and SENP7 are the most divergent members in the SENP family of proteases and they are the only members that bear four loop insertions dispersed throughout their catalytic domains. The superposition of the SENP7 catalytic domain with the SENP2-SUMO complex revealed a tentative SENP7 Loop1-SUMO interface and upon further inspection, distinct residues on SUMO1 and SUMO2 were identified at the interface. A series of mutants were constructed bearing characteristics of both SUMOs and by swapping the residues from SUMO1 to SUMO2 and vice versus we were able to both decrease and increase the activity of the SENP6 and SENP7 toward these substrates. Loop1 SENP6/7 Is Responsible For SUMO Interface Specificity In addition to mutations on SUMO we constructed a series of mutations on SENP7-Loop1 within the tentative SENP7-Loop1-SUMO interface to determine the structural and functional roles of the residues that reside within this region. We were able to recover some of the activity lost by the removal of Loop1 by replacing the four prolines of Loop1 with glycines proving that Loop1 plays at least a structural role in SUMO recognition. We also identified Lys691 of Loop1 in SENP7 as indispensible to the activity of the enzyme. D71 is one of the residues proposed to confer SUMO2/3 specificity in the previous swapping experiments. We mutated this residue in diSUMO2 and saw a decrease in activity of SENP7. This could be explained by our theory that this region on SUMO is interacting with Loop1, more specifically K691, and the decrease in activity was caused by a charge clash between SUMO2 and SENP7 Loop1. To further show the utility of Loop1 in deconjugation of multi-SUMOylated species we inserted the eight residues of SENP6 Loop1 into SENP2. We saw an overall increase in activity of SENP2 against diSUMO2 but not against any other substrate tested. Complexes With Substrates In order to see if SENP6 was able to form any stable complexes in solution, we produced milligram amounts of Δ3SENP6CS and Δ2Δ3SENP6CS (the two constructs of the protein that showed both good yields in protein production and high performance in activity assay). We incubated each protease with SUMO precursors, RanGAP1-SUMO2 and diSUMO2 substrates. Of all the substrates tested, only diSUMO was able to form a stable complex with Δ3SENP6CS and Δ2Δ3SENP6CS. Δ2SENP6CS was also tested but there was no indication of any complex formation, leading to the hypothesis that SENP6 Loop3 was impeding, perhaps entropically, the ability of SENP6 to form a stable complex with diSUMO2. SENP6 Loop3 Characterization Loop3 takes up roughly 40% and 20% of the catalytic domains of SENP6 and SENP7 respectively. In our loop deletion experiments we saw an overall increase in the activity when Loop3 was not present and removal of Loop3 proved vital to the ability of the enzyme to form a stable complex with diSUMO2. In order to try to decipher what role this loop plays in the context of the protease, we isolated the 184 insert from SENP6 and produced and purified the protein. 1-H 1-D NMR pointed to an overall lack of tertiary structure within the loop but limited proteolysis and mass spectrometry analyses showed a stable fragment of around 11kDa. Further circular dichroism and Fourier Transform Infrared Spectroscopy suggested the presence of some secondary structural elements but overall characterization of SENP6 Loop3 showed a mainly unstructured loop.
Books on the topic "SUMO Protease"
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Cheng, Jinke, and Tasneem Bawa-Khalfe. Methods for Reversing Protein Modification: Ubiquitin and SUMO-Specific Proteases. Taylor & Francis Group, 2021.
Find full textBook chapters on the topic "SUMO Protease"
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Tatham, Michael H., and Ronald T. Hay. "FRET-Based In Vitro Assays for the Analysis of SUMO Protease Activities." In Methods in Molecular Biology, 253–68. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-59745-566-4_17.
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Leach, Craig A., Xufan Tian, Michael R. Mattern, and Benjamin Nicholson. "Detection and Characterization of SUMO Protease Activity Using a Sensitive Enzyme-Based Reporter Assay." In Methods in Molecular Biology, 269–81. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-59745-566-4_18.
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Colomina, Neus, Clàudia Guasch, and Jordi Torres-Rosell. "Analysis of SUMOylation in the RENT Complex by Fusion to a SUMO-Specific Protease Domain." In Methods in Molecular Biology, 97–117. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-6502-1_9.
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Yates, Gary, Anjil Srivastava, Beatriz Orosa, and Ari Sadanandom. "Expression, Purification, and Enzymatic Analysis of Plant SUMO Proteases." In Methods in Molecular Biology, 125–33. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3759-2_10.
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Bhagat, Prakash Kumar, Dipan Roy, and Ari Sadanandom. "Expression, Purification, and Enzymatic Analysis of Plant SUMO Proteases." In Methods in Molecular Biology, 109–19. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2784-6_9.
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Reverter, David, and Christopher D. Lima. "Preparation of SUMO Proteases and Kinetic Analysis Using Endogenous Substrates." In Methods in Molecular Biology, 225–39. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-59745-566-4_15.
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Eckhoff, Julia, and R. Jürgen Dohmen. "In Vitro Characterization of Chain Depolymerization Activities of SUMO-Specific Proteases." In Methods in Molecular Biology, 123–35. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-6358-4_9.
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Chachami, Georgia, and Sina-Victoria Barysch. "Comparative SUMO Proteome Analysis Using Stable Isotopic Labeling by Amino Acids (SILAC)." In Methods in Molecular Biology, 71–86. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2863-8_6.
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Cox, Eric, Ijeoma Uzoma, Catherine Guzzo, Jun Seop Jeong, Michael Matunis, Seth Blackshaw, and Heng Zhu. "Identification of SUMO E3 Ligase-Specific Substrates Using the HuProt Human Proteome Microarray." In Methods in Molecular Biology, 455–63. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4939-2550-6_32.
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Besir, Hüseyin. "A Generic Protocol for Purifying Disulfide-Bonded Domains and Random Protein Fragments Using Fusion Proteins with SUMO3 and Cleavage by SenP2 Protease." In Methods in Molecular Biology, 141–54. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-6887-9_9.
Full textConference papers on the topic "SUMO Protease"
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Newmeyer, Allison, Geoffrey Goldberg, and Stewart Hicks. "1968: Cities in Protest." In 109th ACSA Annual Meeting Proceedings. ACSA Press, 2021. http://dx.doi.org/10.35483/acsa.am.109.85.
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This paper chronicles the development of research into the built urban environment and how it guides/empowers/ stifles social interactions during intense moments of politi¬cal upheaval. Beginning with a graduate seminar focused on documenting and representing the spatial progression of protest events in 1968, the research has now grown into a multi-dimensional collaborative investigation with a robust set of discoveries, connections, and lessons. The paper sum¬marizes the goals, methodologies, outcomes, dissemination and future possibilities of the research and speculates on its far-reaching implications and parallels with current events.
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Costa, Graciele Pereira, and DANIELLE PEREIRA COSTA SILVA. "PRINCIPAIS MICROORGANISMOS ENCONTRADOS EM PACIENTES COM INFECÇÕES DO TRATO URINÁRIO (ITU) E MÉTODOS DE DIAGNÓSTICOS UTILIZADOS." In II Congresso Nacional de Microbiologia Clínica On-line. Revista Multidisciplinar em Saúde, 2022. http://dx.doi.org/10.51161/ii-conamic/03.
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Introdução: A infecção do trato urinário (ITU) é considerada um dos problemas clínicos mais comuns e consiste na presença assintomática de bactérias na urina até infecção renal grave. O diagnóstico é considerado muitas vezes difícil clinicamente, sendo necessário a realização de exames de urinálise e cultura urinária ou outros exames para descobrir a origem da infecção. Objetivo: Objetivou-se com a realização deste estudo conhecer os microorganismos mais prevalentes nas infecções urinárias, e delinear os métodos diagnósticos. Material e métodos: O presente estudo trata-se de uma revisão de literatura. As bases de dados utilizadas foram o PubMed, Scientific Eletronic Library Online (SciELO), Medline e refere-se às publicações dos últimos seis anos (2015 a 2021). Resultados: O diagnóstico da infecção do trato urinário é realizado pelo exame clínico e por exames laboratoriais de triagem como o sumário de urina e o diagnóstico confirmatório através do exame de cultura de urina, também conhecida como urocultura, na qual haverá o crescimento e quantificação do microorganismo causador. Uma dificuldade apresentada por este exame é a demora dos resultados, que possuem duração de mais de 24horas. Também se realiza o antibiograma, chamado de Teste de Sensibilidade a Antimicrobianos – TSA, que é essencial para monitorar e conduzir um tratamento adequado e eficiente. Entre os principais microorganismos responsáveis pela ITU, a Escherichia coli é considerada uma das bactérias mais prevalentes, seguida pela Klebsiella pneumoniae e Proteus mirabilis. Conclusão: É grande a quantidade de pacientes com infecção do trato urinário que são tratados com utilização de antibióticos de forma indevida, apresentando resistência bacteriana, sendo assim é de suma importância um diagnóstico eficaz. O diagnóstico da ITU enfrenta um grande desafio e há necessidade de novos exames para utilização em rotinas, principalmente do serviço único de saúde. Também é de suma importância a conscientização dos profissionais para realização de exames conclusivos antes de se realizar a intervenção terapêutica.
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Martins, Claudio Fernando Graciano. "EFEITOS TÓXICOS ASSOCIADOS AO CONSUMO DE CARAMBOLA." In II Congresso Brasileiro de Ciências Biológicas On-line. Revista Multidisciplinar de Educação e Meio Ambiente, 2021. http://dx.doi.org/10.51189/rema/1258.
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Introdução: A carambola (Averrhoa carambola) é uma fruta originária da Ásia, típica de regiões tropicais como o Brasil e fonte de vitaminas e outros nutrientes; a fruta possui ainda em sua composição, o ácido oxálico e a caramboxina. O ácido oxálico apresenta alta nefrotoxicidade podendo levar ao desenvolvimento de Lesão Renal Aguda (LRA) pela deposição de cristais de oxalato de cálcio (pedras nos rins) nos túbulos renais, assim como pela apoptose (morte programada) das células epiteliais tubulares. A caramboxina é uma neurotoxina que pode ser fatal para o paciente com Doença Renal Crônica (DRC), pois com a função renal diminuída, a caramboxina não é eliminada adequadamente pelos rins e sua concentração no sangue aumenta, podendo atravessar a barreira hematoencefálica que protege o sistema nervoso central, levando a manifestações neurológicas, tais como, soluços intratáveis, vômitos, fraqueza muscular, parestesias (formigamento), confusão mental moderada a grave, convulsões, coma e até morte. Objetivos: Informar a comunidade em geral sobre os efeitos tóxicos da carambola em indivíduos com DRC e indivíduos com função renal normal. Material e métodos: Revisão bibliográfica utilizando bases de dados públicas. Resultados: A DRC é identificada como o principal fator de risco para a intoxicação por carambola. Acreditava-se que indivíduos com função renal normal poderia ingerir a fruta sem problemas, mas há relatos na literatura que comprovam que o consumo excessivo da carambola pode levar a LRA. Ainda não se sabe a quantidade máxima recomendada do consumo da carambola em indivíduos sem doença renal prévia, sabe-se que o consumo em grande quantidade (seja fruta ou suco), ou ainda menor quantidade em jejum, deve ser considerado como fator de risco para a toxicidade, já em indivíduos com doença renal, não há quantidade segura do consumo da fruta e, portanto, a carambola deve ser retirada da dieta.Conclusão: Os efeitos tóxicos da carambola podem ser associados não só a complicações em portadores de DRC, mas também naqueles sem doença renal prévia, portanto é importante alertar a população sobre os riscos da ingestão da carambola para o organismo humano.
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Menezes, Rochele Mosmann, VANESSA CAROLINE HERMES, ELIANE CARLOSSO KRUMMENAUER, JANE DAGMAR POLLO RENNER, and MARCELO CARNEIRO. "PERFIL DE SENSIBILIDADE DE BACTÉRIAS GRAM NEGATIVAS EM UMA UTI ADULTO ANTES E DURANTE A PANDEMIA COVID-19." In II Congresso Nacional de Microbiologia Clínica On-line. Revista Multidisciplinar em Saúde, 2022. http://dx.doi.org/10.51161/ii-conamic/46.
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Introdução: As infecções bacterianas estão entre as principais complicações em pacientes internados em Unidades de Terapia Intensiva (UTI), sendo as bactérias gram negativas as principais causadoras de infecções nesses ambientes. Com o surgimento da pandemia do COVID-19 observou-se um aumento da ocorrência de infecções, bem como, um aumento do uso de antimicrobianos, sendo importante um controle frente ao desenvolvimento de resistência. Objetivo: Relacionar o perfil de sensibilidade de bactérias gram negativas prevalentes na Unidade de Terapia Intensiva Adulta de um hospital no interior do Rio Grande do Sul antes e durante a pandemia de COVID-19. Material e métodos: O perfil de sensibilidade das cepas de Pseudomonas spp., Escherichia coli e Grupo CESP (Citrobacter spp, Enterobacter spp., Serratia sp. e Proteus spp.) referentes ao período de janeiro de 2017 a dezembro de 2020 foi coletado através de um banco de dados mantido pela Comissão de Controle de Infecção Hospitalar (CCIH) do hospital. Resultados: Antes da pandemia o perfil de sensibilidade apresentado por Pseudomonas spp. frente Ceftriaxona foi 55% (2017/2018) e 11% (2019) e durante a pandemia apresentou sensibilidade de 100% (2020), já em relação a Piperacilina Tazobactam encontrou-se um perfil de 60% (2017/2018) e 80% (2019) e 100% (2020). Para Escherichia coli encontrou-se uma diminuição no perfil de sensibilidade durante a pandemia frente à Piperacilina Tazobactam 63% (2019/2018), 73% (2019) e 33% (2020) e quanto a Ceftriaxona não houve grandes mudanças no perfil durante a pandemia 43% (2017/2018), 82% (2019) e 83% (2020). Já em relação ao Grupo CESP frente a Ceftriaxona não ocorreram muitas alterações no perfil 42% (2017/2018), 55% (2019) e 50% (2020) assim como frente a Piperacilina Tazobactam 47% (2017/2018), 66% (2019) e 50% (2020). Conclusão: Conhecer o perfil de sensibilidade das bactérias prevalentes na unidade é de suma importância, assim como, as alterações que ocorreram devido a pandemia COVID-19. Felizmente, no hospital em estudo não foram observados grandes mudanças no perfil de sensibilidade, inclusive sendo observado uma melhora deste perfil para alguns microrganismos.
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Lima, Maria Eduarda Barbosa Camilo de, EDILAYNE SILVA DE ALMEIDA, ERICA CAVALCANTE VIEIRA DE GOIS, LUCIANA GESIELLI RODRIGUES ROCHA, and MARIA EDUARDA BARBOSA CAMILO DE LIMA. "IMPORTÂNCIA DO ALEITAMENTO MATERNO NO DESENVOLVIMENTO IMUNOLÓGICO DO RECÉM NASCIDO." In II Congresso Brasileiro de Imunologia On-line. Revista Multidisciplinar em Saúde, 2022. http://dx.doi.org/10.51161/ii-conbrai/6324.
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Introdução: O aleitamento materno fornece todos nutrientes necessários para o desenvolvimento físico, mental e afetivo do recém-nascido, além de estar diretamente ligado ao fortalecimento do sistema imunológico, sendo uma das estratégias mais conhecidas na prevenção de mortes infantis. Além de todos os nutrientes responsáveis pelo crescimento do bebe, o leite materno tem em sua composição células que atuam na defesa do organismo dele, como por exemplo imunoglobulinas que são glicoproteínas responsáveis pela imunidade. As imunoglobulinas presentes no leite materno são IgG, IgA, IgM, IgD e IgE, sendo mais presente o IgA. Apesar dos benefícios mencionados, nem toda mulher deseja ou tem a possibilidade de amamentar, devido a fatores fisiológicos, socioeconômicos ou culturais. Objetivo: Diante dessa problemática objetiva-se demonstrar a importância da amamentação para o desenvolvimento do sistema imunológico do recém-nascido por meio de evidencias cientificas. Material e métodos: A pesquisa será uma revisão integrativa de literatura, realizada por seis etapas: elaboração de pergunta norteadora, busca da literatura, coleta de dados, análise crítica dos estudos incluídos, discussão dos resultados e apresentação da revisão. A busca será realizada no Medical Literature Analysis and Retrieval System Online (MEDLINE), e Literatura Latino-Americana do Caribe em Ciências da Saúde (LILACS) por meio do Portal da Biblioteca Virtual em Saúde (BVS), através da combinação entre os descritores aleitamento materno and sistema imunológico and recém-nascido nos idiomas português e inglês. Serão considerados critérios de inclusão: artigos disponíveis em meio online, de livre acesso no idioma citados, entres os anos 2017 a 2022, que respondam à questão da pesquisa. Serão excluídos relatos de caso, revisões, monografias, dissertações, teses, editoriais e publicações ministeriais. A análise seguirá estrutura descritiva. Resultados: Dentre os resultados obtidos foi perceptível que o aleitamento materno protege o recém-nascido de várias enfermidades como por exemplo das doenças respiratórias, gastrointestinais, infecções alergias, doenças autoimunes, reveste a mucosa intestinal e reduz o índice de mortalidade infantil. Conclusão: Tendo em vista todos os benefícios nutricionais e imunológicos, o aleitamento materno exclusivo é de suma importância e deve ser incentivado até o quarto ou sexto mês de vida do bebe visando a proteção e crescimento do mesmo.
Reports on the topic "SUMO Protease"
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Shamonia, Volodymyr H., Olena V. Semenikhina, Volodymyr V. Proshkin, Olha V. Lebid, Serhii Ya Kharchenko, and Oksana S. Lytvyn. Using the Proteus virtual environment to train future IT professionals. [б. в.], February 2020. http://dx.doi.org/10.31812/123456789/3760.
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Based on literature review it was established that the use of augmented reality as an innovative technology of student training occurs in following directions: 3D image rendering; recognition and marking of real objects; interaction of a virtual object with a person in real time. The main advantages of using AR and VR in the educational process are highlighted: clarity, ability to simulate processes and phenomena, integration of educational disciplines, building an open education system, increasing motivation for learning, etc. It has been found that in the field of physical process modelling the Proteus Physics Laboratory is a popular example of augmented reality. Using the Proteus environment allows to visualize the functioning of the functional nodes of the computing system at the micro level. This is especially important for programming systems with limited resources, such as microcontrollers in the process of training future IT professionals. Experiment took place at Borys Grinchenko Kyiv University and Sumy State Pedagogical University named after A. S. Makarenko with students majoring in Computer Science (field of knowledge is Secondary Education (Informatics)). It was found that computer modelling has a positive effect on mastering the basics of microelectronics. The ways of further scientific researches for grounding, development and experimental verification of forms, methods and augmented reality, and can be used in the professional training of future IT specialists are outlined in the article.
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Ohad, Itzhak, and Himadri Pakrasi. Role of Cytochrome B559 in Photoinhibition. United States Department of Agriculture, December 1995. http://dx.doi.org/10.32747/1995.7613031.bard.
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The aim of this research project was to obtain information on the role of the cytochrome b559 in the function of Photosystem-II (PSII) with special emphasis on the light induced photo inactivation of PSII and turnover of the photochemical reaction center II protein subunit RCII-D1. The major goals of this project were: 1) Isolation and sequencing of the Chlamydomonas chloroplast psbE and psbF genes encoding the cytochrome b559 a and b subunits respectively; 2) Generation of site directed mutants and testing the effect of such mutation on the function of PSII under various light conditions; 3) To obtain further information on the mechanism of the light induced degradation and replacement of the PSII core proteins. This information shall serve as a basis for the understanding of the role of the cytochrome b559 in the process of photoinhibition and recovery of photosynthetic activity as well as during low light induced turnover of the D1 protein. Unlike in other organisms in which the psbE and psbF genes encoding the a and b subunits of cytochrome b559, are part of an operon which also includes the psbL and psbJ genes, in Chlamydomonas these genes are transcribed from different regions of the chloroplast chromosome. The charge distribution of the derived amino-acid sequences of psbE and psbF gene products differs from that of the corresponding genes in other organisms as far as the rule of "positive charge in" is concerned relative to the process of the polypeptide insertion in the thylakoid membrane. However, the sum of the charges of both subunits corresponds to the above rule possibly indicating co-insertion of both subunits in the process of cytochrome b559 assembly. A plasmid designed for the introduction of site-specific mutations into the psbF gene of C. reinhardtii. was constructed. The vector consists of a DNA fragment from the chromosome of C. reinhardtii which spans the region of the psbF gene, upstream of which the spectinomycin-resistance-conferring aadA cassette was inserted. This vector was successfully used to transform wild type C. reinhardtii cells. The spectinomycin resistant strain thus obtained can grow autotrophically and does not show significant changes as compared to the wild-type strain in PSII activity. The following mutations have been introduced in the psbF gene: H23M; H23Y; W19L and W19. The replacement of H23 involved in the heme binding to M and Y was meant to permit heme binding but eventually alter some or all of the electron transport properties of the mutated cytochrome. Tryptophane W19, a strictly conserved residue, is proximal to the heme and may interact with the tetrapyrole ring. Therefore its replacement may effect the heme properties. A change to tyrosine may have a lesser affect on the potential or electron transfer rate while a replacement of W19 by leucine is meant to introduce a more prominent disturbance in these parameters. Two of the mutants, FW19L and FH23M have segregated already and are homoplasmic. The rest are still grown under selection conditions until complete segregation will be obtained. All mutants contain assembled and functional PSII exhibiting an increased sensitivity of PSII to the light. Work is still in progress for the detailed characterization of the mutants PSII properties. A tobacco mutant, S6, obtained by Maliga and coworkers harboring the F26S mutation in the b subunit was made available to us and was characterized. Measurements of PSII charge separation and recombination, polypeptide content and electron flow indicates that this mutation indeed results in light sensitivity. Presently further work is in progress in the detailed characterization of the properties of all the above mutants. Information was obtained demonstrating that photoinactivation of PSII in vivo initiates a series of progressive changes in the properties of RCII which result in an irreversible modification of the RCII-D1 protein leading to its degradation and replacement. The cleavage process of the modified RCII-D1 protein is regulated by the occupancy of the QB site of RCII by plastoquinone. Newly synthesized D1 protein is not accumulated in a stable form unless integrated in reassembled RCII. Thus the degradation of the irreversibly modified RCII-D1 protein is essential for the recovery process. The light induced degradation of the RCII-D1 protein is rapid in mutants lacking the pD1 processing protease such as in the LF-1 mutant of the unicellular alga Scenedesmus obliquus. In this case the Mn binding site of PSII is abolished, the water oxidation process is inhibited and harmful cation radicals are formed following light induced electron flow in PSII. In such mutants photo-inactivation of PSII is rapid, it is not protected by ligands binding at the QB site and the degradation of the inactivated RCII-D1 occurs rapidly also in the dark. Furthermore the degraded D1 protein can be replaced in the dark in absence of light driven redox controlled reactions. The replacement of the RCII-D1 protein involves the de novo synthesis of the precursor protein, pD1, and its processing at the C-terminus end by an unknown processing protease. In the frame of this work, a gene previously isolated and sequenced by Dr. Pakrasi's group has been identified as encoding the RCII-pD1 C-terminus processing protease in the cyanobacterium Synechocystis sp. PCC 6803. The deduced sequence of the ctpA protein shows significant similarity to the bovine, human and insect interphotoreceptor retinoid-binding proteins. Results obtained using C. reinhardtii cells exposes to low light or series of single turnover light flashes have been also obtained indicating that the process of RCII-D1 protein turnover under non-photoinactivating conditions (low light) may be related to charge recombination in RCII due to back electron flow from the semiquinone QB- to the oxidised S2,3 states of the Mn cluster involved in the water oxidation process.