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Relevant bibliographies by topics / Bacterial Small Heat Shock Protein

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Academic literature on the topic 'Bacterial Small Heat Shock Protein'

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Published: 6 September 2023

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Journal articles on the topic "Bacterial Small Heat Shock Protein"

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Bepperling, A., F. Alte, T. Kriehuber, N. Braun, S. Weinkauf, M. Groll, M. Haslbeck, and J. Buchner. "Alternative bacterial two-component small heat shock protein systems." Proceedings of the National Academy of Sciences 109, no. 50 (November 26, 2012): 20407–12. http://dx.doi.org/10.1073/pnas.1209565109.

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Ventura, Marco, Carlos Canchaya, Ziding Zhang, Gerald F. Fitzgerald, and Douwe van Sinderen. "Molecular Characterization of hsp20, Encoding a Small Heat Shock Protein of Bifidobacterium breve UCC2003." Applied and Environmental Microbiology 73, no. 14 (May 18, 2007): 4695–703. http://dx.doi.org/10.1128/aem.02496-06.

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ABSTRACT Small heat shock proteins (sHSPs) are members of a diverse family of stress proteins that are important in cells to protect proteins under stressful conditions. Genome analysis of Bifidobacterium breve UCC2003 revealed a single sHSP-encoding gene, which was classified as a hsp20 gene by comparative analyses. Genomic surveillance of available genome sequences indicated that hsp20 homologs are not widely distributed in bacteria. In members of the genus Bifidobacterium, this gene appears to be present in only 7 of the 30 currently described species. Moreover, phylogenetic analysis using all available bacterial and eukaryotic sHSP sequences revealed a close relationship between bifidobacterial HSP20 and the class B sHSPs found in members of the division Firmicutes. The results of this comparative analysis and variation in codon usage content suggest that hsp20 was acquired by certain bifidobacteria through horizontal gene transfer. Analysis by slot blot, Northern blot, and primer extension experiments showed that transcription of hsp20 is strongly induced in response to severe heat shock regimens and by osmotic shock.

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Whiston, Emily A., Norito Sugi, Merideth C. Kamradt, Coralynn Sack, Susan R. Heimer, Michael Engelbert, Eric F. Wawrousek, Michael S. Gilmore, Bruce R. Ksander, and Meredith S. Gregory. "αB-Crystallin Protects Retinal Tissue during Staphylococcus aureus- Induced Endophthalmitis." Infection and Immunity 76, no. 4 (January 28, 2008): 1781–90. http://dx.doi.org/10.1128/iai.01285-07.

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ABSTRACT Bacterial infections of the eye highlight a dilemma that is central to all immune-privileged sites. On the one hand, immune privilege limits inflammation to prevent bystander destruction of normal tissue and loss of vision. On the other hand, bacterial infections require a robust inflammatory response for rapid clearance of the pathogen. We demonstrate that the retina handles this dilemma, in part, by activation of a protective heat shock protein. During Staphylococcus aureus-induced endophthalmitis, the small heat shock protein αB-crystallin is upregulated in the retina and prevents apoptosis during immune clearance of the bacteria. In the absence of αB-crystallin, mice display increased retinal apoptosis and retinal damage. We found that S. aureus produces a protease capable of cleaving αB-crystallin to a form that coincides with increased retinal apoptosis and tissue destruction. We conclude that αB-crystallin is important in protecting sensitive retinal tissue during destructive inflammation that occurs during bacterial endophthalmitis.

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Large, Andrew T., Martin D. Goldberg, and Peter A. Lund. "Chaperones and protein folding in the archaea." Biochemical Society Transactions 37, no. 1 (January 20, 2009): 46–51. http://dx.doi.org/10.1042/bst0370046.

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A survey of archaeal genomes for the presence of homologues of bacterial and eukaryotic chaperones reveals several interesting features. All archaea contain chaperonins, also known as Hsp60s (where Hsp is heat-shock protein). These are more similar to the type II chaperonins found in the eukaryotic cytosol than to the type I chaperonins found in bacteria, mitochondria and chloroplasts, although some archaea also contain type I chaperonin homologues, presumably acquired by horizontal gene transfer. Most archaea contain several genes for these proteins. Our studies on the type II chaperonins of the genetically tractable archaeon Haloferax volcanii have shown that only one of the three genes has to be present for the organisms to grow, but that there is some evidence for functional specialization between the different chaperonin proteins. All archaea also possess genes for prefoldin proteins and for small heat-shock proteins, but they generally lack genes for Hsp90 and Hsp100 homologues. Genes for Hsp70 (DnaK) and Hsp40 (DnaJ) homologues are only found in a subset of archaea. Thus chaperone-assisted protein folding in archaea is likely to display some unique features when compared with that in eukaryotes and bacteria, and there may be important differences in the process between euryarchaea and crenarchaea.

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Yin, Huaqun, Min Tang, Zhijun Zhou, Xian Fu, Li Shen, Yili Liang, Qian Li, Hongwei Liu, and Xueduan Liu. "Distinctive heat-shock response of bioleaching microorganismAcidithiobacillus ferrooxidansobserved using genome-wide microarray." Canadian Journal of Microbiology 58, no. 5 (May 2012): 628–36. http://dx.doi.org/10.1139/w2012-023.

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Temperature plays an important role in the heap bioleaching. The maldistribution of ventilation in the heap leads to local hyperthermia, which does exert a tremendous stress on bioleaching microbes. In this study, the genome-wide expression profiles of Acidithiobacillus ferrooxidans at 40 °C were detected using the microarray. The results showed that some classic proteases like Lon and small heat-shock proteins were not induced, and heat-inducible membrane proteins were suggested to be under the control of σE. Moreover, expression changes of energy metabolism are noteworthy, which is different from that in heterotrophic bacteria upon heat stress. The induced enzymes catalyzed the central carbon metabolism pathway that might mainly provide precursors of amino acids for protein synthesis. These results will deepen the understanding of the mechanisms of heat-shock response on autotrophic bacteria.

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Zhang, Bo, Sean P. Leonard, Yiyuan Li, and Nancy A. Moran. "Obligate bacterial endosymbionts limit thermal tolerance of insect host species." Proceedings of the National Academy of Sciences 116, no. 49 (November 18, 2019): 24712–18. http://dx.doi.org/10.1073/pnas.1915307116.

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The thermal tolerance of an organism limits its ecological and geographic ranges and is potentially affected by dependence on temperature-sensitive symbiotic partners. Aphid species vary widely in heat sensitivity, but almost all aphids are dependent on the nutrient-provisioning intracellular bacterium Buchnera, which has evolved with aphids for 100 million years and which has a reduced genome potentially limiting heat tolerance. We addressed whether heat sensitivity of Buchnera underlies variation in thermal tolerance among 5 aphid species. We measured how heat exposure of juvenile aphids affects later survival, maturation time, and fecundity. At one extreme, heat exposure of Aphis gossypii enhanced fecundity and had no effect on the Buchnera titer. In contrast, heat suppressed Buchnera populations in Aphis fabae, which suffered elevated mortality, delayed development and reduced fecundity. Likewise, in Acyrthosiphon kondoi and Acyrthosiphon pisum, heat caused rapid declines in Buchnera numbers, as well as reduced survivorship, development rate, and fecundity. Fecundity following heat exposure is severely decreased by a Buchnera mutation that suppresses the transcriptional response of a gene encoding a small heat shock protein. Similarly, absence of this Buchnera heat shock gene may explain the heat sensitivity of Ap. fabae. Fluorescent in situ hybridization revealed heat-induced deformation and shrinkage of bacteriocytes in heat-sensitive species but not in heat-tolerant species. Sensitive and tolerant species also differed in numbers and transcriptional responses of heat shock genes. These results show that shifts in Buchnera heat sensitivity contribute to host variation in heat tolerance.

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Avelange-Macherel, Marie-Hélène, Aurélia Rolland, Marie-Pierre Hinault, Dimitri Tolleter, and David Macherel. "The Mitochondrial Small Heat Shock Protein HSP22 from Pea is a Thermosoluble Chaperone Prone to Co-Precipitate with Unfolding Client Proteins." International Journal of Molecular Sciences 21, no. 1 (December 21, 2019): 97. http://dx.doi.org/10.3390/ijms21010097.

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The small heat shock proteins (sHSPs) are molecular chaperones that share an alpha-crystallin domain but display a high diversity of sequence, expression, and localization. They are especially prominent in plants, populating most cellular compartments. In pea, mitochondrial HSP22 is induced by heat or oxidative stress in leaves but also strongly accumulates during seed development. The molecular function of HSP22 was addressed by studying the effect of temperature on its structural properties and chaperone effects using a recombinant or native protein. Overexpression of HSP22 significantly increased bacterial thermotolerance. The secondary structure of the recombinant protein was not affected by temperature in contrast with its quaternary structure. The purified protein formed large polydisperse oligomers that dissociated upon heating (42 °C) into smaller species (mainly monomers). The recombinant protein appeared thermosoluble but precipitated with thermosensitive proteins upon heat stress in assays either with single protein clients or within complex extracts. As shown by in vitro protection assays, HSP22 at high molar ratio could partly prevent the heat aggregation of rhodanese but not of malate dehydrogenase. HSP22 appears as a holdase that could possibly prevent the aggregation of some proteins while co-precipitating with others to facilitate their subsequent refolding by disaggregases or clearance by proteases.

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Laksanalamai, Pongpan, Dennis L. Maeder, and Frank T. Robb. "Regulation and Mechanism of Action of the Small Heat Shock Protein from the Hyperthermophilic ArchaeonPyrococcus furiosus." Journal of Bacteriology 183, no. 17 (September 1, 2001): 5198–202. http://dx.doi.org/10.1128/jb.183.17.5198-5202.2001.

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ABSTRACT The small heat shock protein (sHSP) from the hyperthermophilePyrococcus furiosus was specifically induced at the level of transcription by heat shock at 105°C. The gene encoding this protein was cloned and overexpressed in Escherichia coli. The recombinant sHSP prevented the majority of E. coli proteins from aggregating in vitro for up to 40 min at 105°C. The sHSP also prevented bovine glutamate dehydrogenase from aggregating at 56°C. Survivability of E. colioverexpressing the sHSP was enhanced approximately sixfold during exposure to 50°C for 2 h compared with the control culture, which did not express the sHSP. Apparently, the sHSP confers a survival advantage on mesophilic bacteria by preventing protein aggregation at supraoptimal temperatures.

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Lupoli, Tania J., Allison Fay, Carolina Adura, Michael S. Glickman, and Carl F. Nathan. "Reconstitution of aMycobacterium tuberculosisproteostasis network highlights essential cofactor interactions with chaperone DnaK." Proceedings of the National Academy of Sciences 113, no. 49 (November 21, 2016): E7947—E7956. http://dx.doi.org/10.1073/pnas.1617644113.

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During host infection,Mycobacterium tuberculosis(Mtb) encounters several types of stress that impair protein integrity, including reactive oxygen and nitrogen species and chemotherapy. The resulting protein aggregates can be resolved or degraded by molecular machinery conserved from bacteria to eukaryotes. Eukaryotic Hsp104/Hsp70 and their bacterial homologs ClpB/DnaK are ATP-powered chaperones that restore toxic protein aggregates to a native folded state. DnaK is essential inMycobacterium smegmatis, and ClpB is involved in asymmetrically distributing damaged proteins during cell division as a mechanism of survival in Mtb, commending both proteins as potential drug targets. However, their molecular partners in protein reactivation have not been characterized in mycobacteria. Here, we reconstituted the activities of the Mtb ClpB/DnaK bichaperone system with the cofactors DnaJ1, DnaJ2, and GrpE and the small heat shock protein Hsp20. We found that DnaJ1 and DnaJ2 activate the ATPase activity of DnaK differently. A point mutation in the highly conserved HPD motif of the DnaJ proteins abrogates their ability to activate DnaK, although the DnaJ2 mutant still binds to DnaK. The purified Mtb ClpB/DnaK system reactivated a heat-denatured model substrate, but the DnaJ HPD mutants inhibited the reaction. Finally, either DnaJ1 or DnaJ2 is required for mycobacterial viability, as is the DnaK-activating activity of a DnaJ protein. These studies lay the groundwork for strategies to target essential chaperone–protein interactions in Mtb, the leading cause of death from a bacterial infection.

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Oliver, Cristian, Patricio Sánchez, Karla Valenzuela, Mauricio Hernández, Juan Pablo Pontigo, Maria C. Rauch, Rafael A. Garduño, Ruben Avendaño-Herrera, and Alejandro J. Yáñez. "Subcellular Location of Piscirickettsia salmonis Heat Shock Protein 60 (Hsp60) Chaperone by Using Immunogold Labeling and Proteomic Analysis." Microorganisms 8, no. 1 (January 15, 2020): 117. http://dx.doi.org/10.3390/microorganisms8010117.

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Piscirickettsia salmonis is the causative bacterial agent of piscirickettsiosis, a systemic fish disease that significantly impacts the Chilean salmon industry. This bacterium possesses a type IV secretion system (T4SS), several proteins of the type III secretion system (T3SS), and a single heat shock protein 60 (Hsp60/GroEL). It has been suggested that due to its high antigenicity, the P. salmonis Hsp60 could be surface-exposed, translocated across the membrane, and (or) secreted into the extracellular matrix. This study tests the hypothesis that P. salmonis Hsp60 could be located on the bacterial surface. Immunogold electron microscopy and proteomic analyses suggested that although P. salmonis Hsp60 was predominantly associated with the bacterial cell cytoplasm, Hsp60-positive spots also exist on the bacterial cell envelope. IgY antibodies against P. salmonis Hsp60 protected SHK-1 cells against infection. Several bioinformatics approaches were used to assess Hsp60 translocation by the T4SS, T3SS, and T6SS, with negative results. These data support the hypothesis that small amounts of Hsp60 must reach the bacterial cell surface in a manner probably not mediated by currently characterized secretion systems, and that they remain biologically active during P. salmonis infection, possibly mediating adherence and (or) invasion.

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Dissertations / Theses on the topic "Bacterial Small Heat Shock Protein"

1

Studer, Sonja. "Chaperone activity and oligomerization of bacterial small heat shock proteins /." [S.l.] : [s.n.], 2002. http://e-collection.ethbib.ethz.ch/show?type=diss&nr=14550.

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Collier, Miranda. "Small heat shock protein interactions with in vivo partners." Thesis, University of Oxford, 2018. http://ora.ox.ac.uk/objects/uuid:24cf8041-c82d-4bc4-87a7-0ae7e38f1879.

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Small heat-shock proteins (sHsps) are part of a broad cellular sys- tem that functions to maintain a stable proteome under stress. They also perform a variety of regulatory roles at physiological conditions. Despite the multitude of sHsp targets, their interactions with partners are not well understood due to highly dynamical structures. In this thesis, I apply a variety of biophysical and structural approaches to examine distinct interactions made by the abundant human sHsps αβ-crystallin and Hsp27. First, I find that αβ-crystallin binds a cardiac-specific domain of the muscle sarcomere protein titin. A cardiomyopathy-causative variant of αβ-crystallin is shown to disrupt this interaction, with demonstrated implications for tissue biomechanics. Next, I investigate the conformation and unfolding behaviour of another sarcomere-associated protein, filamin C, finding support for the hypothesis that it is mechanosensitive. This leads into an interrogation of the interaction between filamin C and Hsp27, which we find is modulated by phosphorylation of Hsp27. This modulation only manifests during filamin C unfolding, pointing toward a protective chaperoning mode against over-extension during mechanical stress. This finding is bolstered by up-regulation and interaction of both proteins in a mouse model of heart failure. I establish a system for similar studies of a third sHsp, cvHsp, which is muscle-specific and implicated in various myopathies but scantly understood at the molecular level compared to αβ-crystallin and Hsp27. Finally, I probe the stoichiometries and kinetics of complexes formed between αβ-crystallin and Hsp27 themselves, which co-assemble into a highly polydisperse ensemble. This involved the development of a high-resolution native mass spectrometry method for disentangling heterogeneous systems. Together these findings add to our understanding of the roles and mechanisms of ATP-independent molecular chaperones.

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Franzmann, Titus Marcellus. "Chaperone mechanism of the small heat shock protein Hsp26." kostenfrei, 2008. http://mediatum2.ub.tum.de/doc/652224/652224.pdf.

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Sund, Derrick T. "Replica Exchange Molecular Dynamics of a Small Heat Shock Protein." Thesis, The University of Arizona, 2011. http://hdl.handle.net/10150/144990.

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Morris, Amie Michelle. "Structure and function of the mammalian small heat shock protein Hsp25." Access electronically Access electronically, 2007. http://www.library.uow.edu.au/adt-NWU/public/adt-NWU20080605.104334/index.html.

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6

Carson, Kenneth Harris. "Study and characterization of a novel small heat shock protein from Babesia." [College Station, Tex. : Texas A&M University, 2006. http://hdl.handle.net/1969.1/ETD-TAMU-1813.

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7

di, Bard Barbara Lelj Garolla. "Self-association and chaperon activity of the small heat shock protein 27." Thesis, University of British Columbia, 2007. http://hdl.handle.net/2429/31382.

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Human Hsp27 is a member of the small heat shock protein family that is over-expressed during cellular stress and that is involved in biological functions ranging from inhibition of apoptosis to regulation of cellular glutathione levels. In addition, Hsp27 is an ATP-independent molecular chaperon that binds to unfolding peptides and inhibits their precipitation. Roles for Hsp27 in several human diseases have also been proposed. For example, the expression of Hsp27 by several human tumors has been noted as a potential diagnostic feature or a therapeutic target. Increasing evidence indicates that the biological functions of Hsp27 are linked to the reversible self-association of the protein to form large oligomers in a process that is at least in part regulated by reversible phosphorylation of three Ser residues. The three-dimensional structure of Hsp27 is not available, and relatively few rigorous physical studies of the protein have been reported. In the present study, analytical ultracentrifugation has been used to define self-association of Hsp27 and selected variants as a function of protein concentration, pH, temperature, and ionic strength to evaluate the role of structural domains believed to be functionally significant. These results are correlated with the chaperon activity, as determined by monitoring the inhibition of insulin unfolding, and with the kinetics of subunit exchange, monitored by fluorescence resonance energy transfer. The results establish that wild-type Hsp27 forms a distribution of oligomers that ranges from dimers to at least 32-mers and that oligomerization is highly regulated by temperature but not ionic strength or pH. Moreover, the oligomeric size of Hsp27 increases with increased temperature in a manner that correlates well with increased chaperon activity and rate of subunit exchange. Comparison of results from all three types of experiments obtained for the wild-type protein to those obtained with Hsp27 variants has led to the development of a model for Hsp27 self-association and chaperon activity.
Medicine, Faculty of
Biochemistry and Molecular Biology, Department of
Graduate

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8

Dabbaghizadeh, Afrooz. "Structure and function of mitochondrial small heat shock protein 22 in Drosophila melanogaster." Doctoral thesis, Université Laval, 2018. http://hdl.handle.net/20.500.11794/34491.

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Les petites protéines de choc thermique (sHsps) ont été découvertes initialement chez Drosophila. Les membres de cette famille sont des chaperons moléculaires sont présentsdans la plupart des organismes eucaryotes et procaryotes et certains virus. En plus d’être induites en réponse à la plupart des stresseurs dont un choc thermique, elles sont également exprimés en absence de stress. Les sHsps forment des structures dynamiques s'assemblant en oligomères et elles sont essentielles durant les conditions de stress en empêchant l'agrégation des protéines dénaturées et en favorisant leur repliement par des chaperons moléculaires dépendants de l'ATP. Le génome de Drosophila melanogastercode pour 12 sHsp, qui ont des profils d'expression développementaux, des localisations intracellulaires diverses et des spécificités de substrats distincts. DmHsp22 est jusqu'à présent la seule sHsp localisée dans les mitochondries avant et après un choc thermique. Elle est préférentiellement régulée lors du vieillissement et en réponse à la chaleur et aux stress oxydants. La surexpression de DmHsp22 augmente la durée de vie et la résistance au stress et sa régulation négative est préjudiciable. C'est un chaperon efficace, qui pourrait être impliqué dans la réponse mitochondriale au dépliement protéique (UPRMT). Cependant, le mécanisme exact de son action est mal compris. Structurellement, DmHsp22 forme une population d'oligomères semblable aux nombreux sHsps de métazoaires et différente deDmHsp27. L'alignement des séquences de la région ACDde DmHsp22 avec des sHsp de drosophile et d'autres organismes a démontré la présence de trois résidus d'arginine hautement conservés dans ce domaine. Une forte conservationde ces résidus suggère leur implication possible dans la structure et la fonction de DmHsp22. La substitution des résidus d'arginine hautement conservés dans les sHsps de mammifères est associée à certaines pathogenèses et déclenche des changements de conformation des protéines ainsi que l'agrégation des protéines intracellulaires. La mutation de l'arginine en glycine au niveau de trois résidus hautement conservés d'ACD dans DmHsp22 (R105, R109, R110) résulte en une population oligomérique qui, dans le cas de R110G, perturbe la structure et provoque la formation de petits oligomères. Bien que DmHsp22 ainsi que les mutants aient été caractérisés comme des chaperons efficaces in vitro, les mécanismes d'action exacts dans les mitochondries et l'information sur le comportement protecteur nécessitent la détermination du réseau d’interaction in vivo. Nous avons utilisé la technique capture d’immunoaffinité (CIA) pour récupérer 60 protéines qui interagissent spécifiquement avec DmHsp22 in vivo pendant le traitement normal et thermique, dans le surnageant des cellules de mammifères exprimant la DmHsp22. L’CIA effectuée sur la fraction mitochondriale a permis d’identifies 39 protéines qui interagissent spécifiquement avec DmHsp22. La combinaison de l’IAC avec l'analyse par spectroscopie de masse de mitochondries de cellules HeLa transfectées avec DmHsp22 a conduit à l'identification de partenaires de liaison à DmHsp22 dans des conditions de normales et de choc thermique. L'interaction entre DmHsp22 et deux autres chaperons mitochondriaux a été validée par immunobuvardage. Notre approche a montré que les cellules HeLa exprimant DmHsp22 augmentent la consommation d'oxygène mitochondrial et les teneurs en ATP, ce qui confère un nouveau rôle à DmHsp22 dans les mitochondries. En outre, l'activité d’une luciférase exogène a légèrement augmenté dans les cellules HeLa exprimant DmHsp22 après que l'activité enzymatique ait été réduite à la suite de l'exposition à la chaleur. En résumé, ce projet a permis de caractériser la structure oligomérique de DmHsp22 et un certain nombre de mutants dans le domaine alpha cristallin tout en fournissant un rôle potentiel mécanistique dans l’homéostase mitochondriale. La détermination du réseau mitochondrial de DmHsp22 suggère son importance dans cette organelle non seulement en tant que chaperon moléculaire, mais aussi en tant que protéine impliquée dans plusieurs fonctions cellulaires significatives.
The small heat shock proteins (sHsps) were first discovered in Drosophila. Members of this family are molecular chaperones and are present in most eukaryotic and prokaryotic. Although, they are induced in response to most of the stressors including heat shock, they are also expressed in absence of stress. SHsps for mdynamic structures that assemble into oligomers which are essential during stress conditions by preventing aggregation of denatured proteins and promoting their folding by ATP dependent molecular chaperones. Drosophila melanogaster genome encodes 12 sHsps, that have developmental expression patterns, diverse intracellular localizations and distinct substrate specificities. DmHsp22 is up to now the only sHsp localized in mitochondria before and after heat shock. It is preferentially regulated during ageing and in response to heat and oxidative stresses. Over-expression of DmHsp22 increases lifespan and resistance to stress and its down-regulation is detrimental. It is an efficient chaperone and could be involved in the mitochondrial unfolding protein response (UPRMT). However, the exact mechanism of its action is poorly understood. Structurally, DmHsp22 forms one population of oligomers similar to the many metazoan sHsps but DmHsp27. Sequence alignment of DmHsp22 with sHsps in Drosophilaand other organisms at the alpha crystalline domain (ACD) region demonstrated the presence of three highly conserved arginine residues in this domain. Strong conservation of these residues suggest their possible involvement in structure and function of DmHsp22. Substitution of highly conserved arginine residues in mammalian sHsps is associated with some pathogenesis and triggers protein conformational changes as well as intracellular protein aggregation. Mutation of arginine to glycine at three highly conserved residues of ACD in DmHsp22 (R105, R109, R110) results in one oligomeric population as well which in the case of R110G disrupts the structure and causes formation of smaller oligomers. Although DmHsp22 as well as mutants have been characterized as effective in vitro chaperones, the exact mechanism(s) of action in mitochondria and information about protective behavior requires defining of in vivoprotein interacting network. We have used immunoaffinity conjugation (IAC) technique to recover 60 proteins that specifically interact with DmHsp22 in vivo during normal and heat treatment using cell extract of mammalian cells expressing DmHsp22. The IAC performed on mitochondrial fraction identified 39 proteins that specifically interact with DmHsp22. Combination of IAC with mass spectroscopy analysis of mitochondria of HeLa cells transfected with DmHsp22 resulted in identification of DmHsp22-binding partners under normal andunder heat shock conditions. Interaction between DmHsp22 and two other mitochondrial chaperones was validated by immunoblotting. Our approach showed that HeLa cells expressing DmHsp22 increase maximal mitochondrial oxygen consumption and ATP contents which provides a new mechanistic role for DmHsp22 in mitochondria. Further more, exogenous luciferase activity slightly increased in HeLa cells expressing DmHsp22 after the enzyme activity reduced as a result of exposure to heat. In summary, this project has characterized the oligomeric structure of DmHsp22 and a number of mutants inthe alpha crystalline domain while providing a potential mechanistic role in mitochondrial homeostasis. Determining mitochondrial network of DmHsp22 suggest its importance in this organelle not only as a molecular chaperone but also as a protein involved in several significant cellular functions.

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Friedrich, Kenneth Lane. "Dynamic behavior of small heat shock protein subunits and their interactions with substrates." Diss., The University of Arizona, 2003. http://hdl.handle.net/10150/280410.

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Small heat shock proteins (sHsps) are oligomeric proteins expressed by cells in response to high temperatures. It is believed that sHsps are produced as a defensive mechanism against temperature stress and act as molecular chaperones by binding and protecting heat-labile proteins from irreversible aggregation. Binding results in the formation of sHsp/substrate complexes from which substrate can later be refolded by ATP-dependent chaperones. Despite past investigations, many aspects of this model remain poorly defined. Results presented here provide new insight into the mechanism of sHsp action. sHsp chaperone activity and sHsp oligomerization are closely linked. Therefore, an understanding of the oligomeric structure, subunit number, and subunit dynamics is essential to understanding sHsp action. Three sHsps were analyzed for these properties: PsHsp18.1 from pea, TaHsp16.9 from wheat, and SynHsp16.6, from the cyanobacterium Synechocystis. In solution, SynHsp16.6 is a duodecamer, while TaHsp16.9 and PsHsp18.1 are dodecamers. An equilibrium between an oligomeric and suboligomeric state was observed for PsHsp18.1 and SynHsp16.6. Increasing temperatures resulted in the reversible dissociation of the TaHsp16.9 oligomer into a suboligomeric species. These results indicate that subunit dynamics are important for sHsp function. Interactions between sHsp and substrate in sHsp/substrate complexes and the mechanism by which substrate is transferred to refolding chaperones are poorly defined. C-terminal affinity-tagged sHsps were used to investigate these issues. This analysis revealed that while some sHsp subunits within sHsp/substrate complexes remain dynamic, complex size remains unchanged and association of substrate with sHsp is not similarly dynamic. These data suggest a model in which ATP-dependent chaperones associate directly with sHsp-bound substrate to initiate refolding. The homologous TaHsp16.9 and PsHsp18.1 are structurally similar. However, TaHsp16.9 interacts differently with substrate and is less effective at protecting substrate than PsHsp18.1. Studies with chimeric sHsps made between PsHsp18.1 and TaHsp16.9 revealed that the N-terminal arm is involved in subunit affinity, substrate protection, and substrate refolding, but interactions between the N-terminal arm and C-terminal domain are also critical for these aspects of chaperone activity. Additionally, the first ten residues of the N-terminal arm play a role in sHsp subunit affinity and substrate protection, but are unimportant for substrate protection.

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10

Muchowski, Paul J. "Structural and functional characterization of human alphaB-crystallin, a small heat-shock protein and molecular chaperone /." Thesis, Connect to this title online; UW restricted, 1998. http://hdl.handle.net/1773/5676.

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Books on the topic "Bacterial Small Heat Shock Protein"

1

Ramage, Judith Margaret. Immunological memory: T cell responses to bacterial heat shock protein 60. Birmingham: University of Birmingham, 1997.

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Kegel, Kimberly Beth. Small heat shock protein αB-crystallin: Functional analysis during hypertonic stress. 1997.

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Book chapters on the topic "Bacterial Small Heat Shock Protein"

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Chang, Zengyi. "Understanding What Small Heat Shock Proteins Do for Bacterial Cells." In Heat Shock Proteins, 511–25. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-16077-1_22.

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Haslbeck, Martin. "Small Heat Shock Proteins in Bacteria." In Stress and Environmental Regulation of Gene Expression and Adaptation in Bacteria, 747–53. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2016. http://dx.doi.org/10.1002/9781119004813.ch71.

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Brötz-Oesterhelt, Heike, and Peter Sass. "Bacterial Cell Stress Protein ClpP: A Novel Antibiotic Target." In Heat Shock Proteins, 375–85. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-6787-4_24.

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Voellmy, R., Y. Luo, R. Mestril, J. Amin, and J. Ananthan. "Mechanisms of Regulation of Small Heat Shock Protein Genes in Drosophila." In Heat Shock, 35–42. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76679-4_4.

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Boelens, Wilbert C. "Role of Small Heat Shock Protein HspB5 in Cancer." In Heat Shock Proteins, 301–14. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-16077-1_12.

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Barth, Holger. "Role of Peptidyl-Prolyl cis/trans Isomerases in Cellular Uptake of Bacterial Protein Toxins." In Heat Shock Proteins, 251–65. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-6787-4_16.

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Török, Zsolt, Ana-Maria Pilbat, Imre Gombos, Enikö Hocsák, Balázs Sümegi, Ibolya Horváth, and László Vígh. "Evidence on Cholesterol-Controlled Lipid Raft Interaction of the Small Heat Shock Protein HSPB11." In Heat Shock Proteins, 75–85. Dordrecht: Springer Netherlands, 2012. http://dx.doi.org/10.1007/978-94-007-4740-1_5.

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Härndahl, Ulrika, Niklas Gustavsson, Roberta Buffoni, Janet F. Bornman, Carin Jarl-Sunesson, and Cecilia Sundby. "The Chloroplast Small Heat Shock Protein in Transgenic Arabidopsis Thaliana." In Photosynthesis: Mechanisms and Effects, 2461–64. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-3953-3_576.

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Norris, Carol E., and Lawrence E. Hightower. "Discovery of Two Distinct Small Heat Shock Protein (HSP) Families in the Desert Fish Poeciliopsis." In Small Stress Proteins, 19–35. Berlin, Heidelberg: Springer Berlin Heidelberg, 2002. http://dx.doi.org/10.1007/978-3-642-56348-5_2.

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Osteryoung, Katherine W., Brian Pipes, Nadja Wehmeyer, and Elizabeth Vierling. "Studies of a Chloroplast-Localized Small Heat Shock Protein in Arabidopsis." In Biochemical and Cellular Mechanisms of Stress Tolerance in Plants, 97–113. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-79133-8_5.

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Conference papers on the topic "Bacterial Small Heat Shock Protein"

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Doseff, AI, OH Voss, and ME Gonzalez-Mejia. "The Small Heat Shock Protein 27 Regulates Monocyte/Macrophage Survival and Differentiation." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a1354.

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Kwon, Jin-Sun, An-Na Moon, Joon-Tae Park, Soo-Jung Hong, Jin-Ah Jeong, Sung-Wook Kwon, Myong-Jae Lee, et al. "Abstract 2768: IDH1057, A novel, synthetic, small molecule inhibitor of heat shock protein 90(Hsp90)." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-2768.

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Balaburski, Gregor M., Julie Leu, Seth A. Hayik, Mark Andrake, Roland Dunbrack, Donna George, and Maureen E. Murphy. "Abstract 3771: Identification of novel small molecule inhibitors of the inducible heat shock protein Hsp70." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-3771.

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Hendrix, A., D. Maynard, P. Pauwels, G. Braems, H. Denys, R. Van den Broecke, S. Van Belle, et al. "The Secretory Small GTPase Rab27B Regulates Invasive Tumor Growth and Metastasis through Extracellular Heat Shock Protein 90α." In Abstracts: Thirty-Second Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 10‐13, 2009; San Antonio, TX. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/0008-5472.sabcs-09-6144.

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Chen, Hongpeng, Xiaofeng Tan, and Fangming Hu. "Cloning, Bioinformatics Analysis and Functional Identification of a Novel Small Heat Shock Protein Gene from Camellia oleifera Seed." In 2009 3rd International Conference on Bioinformatics and Biomedical Engineering (iCBBE). IEEE, 2009. http://dx.doi.org/10.1109/icbbe.2009.5162514.

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Taldone, Tony, Pallav D. Patel, Yanlong Kang, Anna Rodina, Tanaji T. Talele, and Gabriela Chiosis. "Abstract 3895: Rational design of small molecule inhibitors that bind to an allosteric pocket on human heat shock protein 70 (Hsp70)." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-3895.

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Dong, H., X. Wan, J. Zhang, C. Ye, W. Zhong, and S. Cai. "Targeting Extracellular Heat Shock Protein 90α to Overcome Resistance to Gefitinib in Non Small Cell Lung Cancer via Epithelial to Mesenchymal Transition." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a3963.

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Kim, Kyeong Kyu, Joohyun Lee, Truc Kim, and Bum Han Ryu. "High resolution cryo-EM structure of the <em>Methanocaldococcus jannaschii </em>small-heat shock protein." In The 3rd International Online Conference on Crystals. Basel, Switzerland: MDPI, 2022. http://dx.doi.org/10.3390/iocc_2022-12141.

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Kim, Kyeong Kyu, Joohyun Lee, Truc Kim, and Bum Han Ryu. "High resolution cryo-EM structure of the <em>Methanocaldococcus jannaschii </em>small-heat shock protein." In The 3rd International Online Conference on Crystals. Basel, Switzerland: MDPI, 2022. http://dx.doi.org/10.3390/iocc_2022-12141.

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Lee, SunHwa, Soyeon Kim, Tae Min Kim, Dong-Wan Kim, and Dae Seog Heo. "Abstract 3272: Differential sensitivities to heat shock protein 90(HSP90) inhibitors in anaplastic lymphoma kinase(ALK)-positive non-small cell ling cancer(NSCLC) cells." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-3272.

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Reports on the topic "Bacterial Small Heat Shock Protein"

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Hiremath, Shiv, Kirsten Lehtoma, and Gopi K. Podila. Identification of a small heat-shock protein associated with a ras-mediated signaling pathway in ectomycorrhizal symbiosis. Newtown Square, PA: U.S. Department of Agriculture, Forest Service, Northern Research Station, 2009. http://dx.doi.org/10.2737/nrs-rp-7.

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