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Academic literature on the topic 'NUBP1'

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Published: 10 March 2023

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Journal articles on the topic "NUBP1"

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Okuno, Takashi, Hiroko Yamabayashi, and Kentaro Kogure. "Comparison of intracellular localization of Nubp1 and Nubp2 using GFP fusion proteins." Molecular Biology Reports 37, no. 3 (March 5, 2009): 1165–68. http://dx.doi.org/10.1007/s11033-009-9477-7.

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Kypri, Elena, Andri Christodoulou, Giannis Maimaris, Mette Lethan, Maria Markaki, Costas Lysandrou, Carsten W. Lederer, et al. "The nucleotide-binding proteins Nubp1 and Nubp2 are negative regulators of ciliogenesis." Cellular and Molecular Life Sciences 71, no. 3 (June 27, 2013): 517–38. http://dx.doi.org/10.1007/s00018-013-1401-6.

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Christodoulou, A. "Motor protein KIFC5A interacts with Nubp1 and Nubp2, and is implicated in the regulation of centrosome duplication." Journal of Cell Science 119, no. 10 (May 15, 2006): 2035–47. http://dx.doi.org/10.1242/jcs.02922.

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Stehling, Oliver, Daili J. A. Netz, Brigitte Niggemeyer, Ralf Rösser, Richard S. Eisenstein, Helene Puccio, Antonio J. Pierik, and Roland Lill. "Human Nbp35 Is Essential for both Cytosolic Iron-Sulfur Protein Assembly and Iron Homeostasis." Molecular and Cellular Biology 28, no. 17 (June 23, 2008): 5517–28. http://dx.doi.org/10.1128/mcb.00545-08.

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ABSTRACT The maturation of cytosolic iron-sulfur (Fe/S) proteins in mammalian cells requires components of the mitochondrial iron-sulfur cluster assembly and export machineries. Little is known about the cytosolic components that may facilitate the assembly process. Here, we identified the cytosolic soluble P-loop NTPase termed huNbp35 (also known as Nubp1) as an Fe/S protein, and we defined its role in the maturation of Fe/S proteins in HeLa cells. Depletion of huNbp35 by RNA interference decreased cell growth considerably, indicating its essential function. The deficiency in huNbp35 was associated with an impaired maturation of the cytosolic Fe/S proteins glutamine phosphoribosylpyrophosphate amidotransferase and iron regulatory protein 1 (IRP1), while mitochondrial Fe/S proteins remained intact. Consequently, huNbp35 is specifically involved in the formation of extramitochondrial Fe/S proteins. The impaired maturation of IRP1 upon huNbp35 depletion had profound consequences for cellular iron metabolism, leading to decreased cellular H-ferritin, increased transferrin receptor levels, and higher transferrin uptake. These properties clearly distinguished huNbp35 from its yeast counterpart Nbp35, which is essential for cytosolic-nuclear Fe/S protein assembly but plays no role in iron regulation. huNbp35 formed a complex with its close homologue huCfd1 (also known as Nubp2) in vivo, suggesting the existence of a heteromeric P-loop NTPase complex that is required for both cytosolic Fe/S protein assembly and cellular iron homeostasis.
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Stehling, Oliver, Jae-Hun Jeoung, Sven A. Freibert, Viktoria D. Paul, Sebastian Bänfer, Brigitte Niggemeyer, Ralf Rösser, Holger Dobbek, and Roland Lill. "Function and crystal structure of the dimeric P-loop ATPase CFD1 coordinating an exposed [4Fe-4S] cluster for transfer to apoproteins." Proceedings of the National Academy of Sciences 115, no. 39 (September 10, 2018): E9085—E9094. http://dx.doi.org/10.1073/pnas.1807762115.

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Maturation of iron-sulfur (Fe-S) proteins in eukaryotes requires complex machineries in mitochondria and cytosol. Initially, Fe-S clusters are assembled on dedicated scaffold proteins and then are trafficked to target apoproteins. Within the cytosolic Fe-S protein assembly (CIA) machinery, the conserved P-loop nucleoside triphosphatase Nbp35 performs a scaffold function. In yeast, Nbp35 cooperates with the related Cfd1, which is evolutionary less conserved and is absent in plants. Here, we investigated the potential scaffold function of human CFD1 (NUBP2) in CFD1-depleted HeLa cells by measuring Fe-S enzyme activities or 55Fe incorporation into Fe-S target proteins. We show that CFD1, in complex with NBP35 (NUBP1), performs a crucial role in the maturation of all tested cytosolic and nuclear Fe-S proteins, including essential ones involved in protein translation and DNA maintenance. CFD1 also matures iron regulatory protein 1 and thus is critical for cellular iron homeostasis. To better understand the scaffold function of CFD1-NBP35, we resolved the crystal structure of Chaetomium thermophilum holo-Cfd1 (ctCfd1) at 2.6-Å resolution as a model Cfd1 protein. Importantly, two ctCfd1 monomers coordinate a bridging [4Fe-4S] cluster via two conserved cysteine residues. The surface-exposed topology of the cluster is ideally suited for both de novo assembly and facile transfer to Fe-S apoproteins mediated by other CIA factors. ctCfd1 specifically interacted with ATP, which presumably associates with a pocket near the Cfd1 dimer interface formed by the conserved Walker motif. In contrast, ctNbp35 preferentially bound GTP, implying differential regulation of the two fungal scaffold components during Fe-S cluster assembly and/or release.
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Schnatwinkel, Carsten, and Lee Niswander. "Nubp1 Is Required for Lung Branching Morphogenesis and Distal Progenitor Cell Survival in Mice." PLoS ONE 7, no. 9 (September 17, 2012): e44871. http://dx.doi.org/10.1371/journal.pone.0044871.

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Ververis, Antonis, Andri Christodoulou, Maria Christoforou, Christina Kamilari, Carsten W. Lederer, and Niovi Santama. "A novel family of katanin-like 2 protein isoforms (KATNAL2), interacting with nucleotide-binding proteins Nubp1 and Nubp2, are key regulators of different MT-based processes in mammalian cells." Cellular and Molecular Life Sciences 73, no. 1 (July 8, 2015): 163–84. http://dx.doi.org/10.1007/s00018-015-1980-5.

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Nakashima, Hiroshi, Marija J. Grahovac, Richard Mazzarella, Hiroyuki Fujiwara, John R. Kitchen, Tracy A. Threat, and Minoru S. H. Ko. "Two Novel Mouse Genes—Nubp2, Mapped to the t-Complex on Chromosome 17, and Nubp1, Mapped to Chromosome 16— Establish a New Gene Family of Nucleotide-Binding Proteins in Eukaryotes." Genomics 60, no. 2 (September 1999): 152–60. http://dx.doi.org/10.1006/geno.1999.5898.

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Camponeschi, Francesca, Nihar Ranjan Prusty, Sabine Annemarie Elisabeth Heider, Simone Ciofi-Baffoni, and Lucia Banci. "GLRX3 Acts as a [2Fe–2S] Cluster Chaperone in the Cytosolic Iron–Sulfur Assembly Machinery Transferring [2Fe–2S] Clusters to NUBP1." Journal of the American Chemical Society 142, no. 24 (May 20, 2020): 10794–805. http://dx.doi.org/10.1021/jacs.0c02266.

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Guarascio, Rosellina, Dervis Salih, Marina Yasvoina, Frances A. Edwards, Michael E. Cheetham, and Jacqueline van der Spuy. "Negative Regulator of Ubiquitin-Like Protein 1 modulates the autophagy–lysosomal pathway via p62 to facilitate the extracellular release of tau following proteasome impairment." Human Molecular Genetics 29, no. 1 (November 6, 2019): 80–96. http://dx.doi.org/10.1093/hmg/ddz255.

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Abstract Negative regulator of ubiquitin-like protein 1 (NUB1) and its longer isoform NUB1L are ubiquitin-like (UBL)/ubiquitin-associated (UBA) proteins that facilitate the targeting of proteasomal substrates, including tau, synphilin-1 and huntingtin. Previous data revealed that NUB1 also mediated a reduction in tau phosphorylation and aggregation following proteasome inhibition, suggesting a switch in NUB1 function from targeted proteasomal degradation to a role in autophagy. Here, we delineate the mechanisms of this switch and show that NUB1 interacted specifically with p62 and induced an increase in p62 levels in a manner facilitated by inhibition of the proteasome. NUB1 moreover increased autophagosomes and the recruitment of lysosomes to aggresomes following proteasome inhibition. Autophagy flux assays revealed that NUB1 affected the autophagy–lysosomal pathway primarily via the UBA domain. NUB1 localized to cytosolic inclusions with pathological forms of tau, as well as LAMP1 and p62 in the hippocampal neurons of tauopathy mice. Finally, NUB1 facilitated the extracellular release of tau following proteasome inhibition. This study thus shows that NUB1 plays a role in regulating the autophagy–lysosomal pathway when the ubiquitin proteasome system is compromised, thus contributing to the mechanisms targeting the removal of aggregation-prone proteins upon proteasomal impairment.
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Dissertations / Theses on the topic "NUBP1"

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Tan, Ka-Liong. "Translational relevance of AIPL1 and NUB1 in cancer." Thesis, University of Oxford, 2017. https://ora.ox.ac.uk/objects/uuid:9b0e5061-bf81-4006-af9e-5018f113cb97.

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Background: Aryl Hydrocarbon Receptor Interacting Protein-Like 1 (AIPL1) interacts with NUB1 and restricts the entry of NUB1 protein into the nucleus. The interferon-induced NEDD8 ultimate buster (NUB1) protein causes degradation of neddylated and FAT10ylated proteins through the ubiquitin proteasome system. We observed AIPL1 were frequently down-regulated in various cancers compared to normal tissues. The mechanistic roles of AIPL1 and NUB1 protein in cancer cell cycle regulation remain unexplored. Results: Meta-analysis of cancer databases revealed that expression transcripts of chaperones, including AIPL1, were down-regulated in lung, pancreatic cancer and breast cancer relative to the adjacent normal tissues. Opposite levels of both AIPL1 and NUB1 transcripts were observed in the breast cancer. So it triggers the in vitro experiments using breast cancer cells. METABRIC breast cancer clinical cohort highlighted that patients with low NUB1 transcripts had poor survival in the ER-negative subgroup (but not in ER-positive) of breast cancer patients: hazard ratio (HR)=0.66, 95% confidence interval (CI)=0.5-0.87, p=0.003 and triple negative subgroup of breast cancer patients: HR=0.67, 95% CI=0.47-0.96, p=0.028. NUB1 silencing significantly inhibits in vitro cell growth in MDA-MB-231 and MCF7 under hypoxia. AIPL1 protein forms multimers in cancer cells. NUB1 protein moved into the nucleus in hypoxia (0.1% O2 48hrs) with final confluency at 80-90%. p21 (marker of senescence) & p27 (marker of cell cycle arrest) accumulated in NUB1-silent MDA-MB-231 and RCC4 cells. It suggested that low NUB1 nuclear localisation in hypoxia cause cancer cell cycle arrest. In MDA-MB-231 cell, upon hypoxia, neddylation inhibitor (MLN4924) treated and siNUB1 transfected cells showed decreased CUL1 and further accumulated p21 & p27. The evidence suggested lower neddylated CUL1 and reduced NUB1 cooperatively stabilise p21 and p27 as the substrate of CUL1-ubiquitin ligase. The neddylation inhibitor MLN4924 treated and NUB1 knockdown group exhibited more cells in sub-G1 stage as compared to the control group. In connection to higher p21/p27, it is associated with prolonged arrested cellular aging with depletion. After silencing of NUB1, the increases in cell death of cancer cells upon hypoxia happen through the neddylation-dependent CUL1-p27-p21 and CUL2-VHL axis. We then demonstrated that HIF1α protein could be both neddylated and FAT10ylated upon reoxygenation. In a tissue microarray study of breast cancer, lower cytoplasmic expression (n=57) had worse overall survival than higher cytoplasmic expression (n=57): HR=1.779, 95% CI=1.006-3.346, p=0.048. Conclusions: AIPL1 and NUB1 proteins exert a role in cell cycle regulation in breast cancer. Low cytoplasmic NUB1 levels are observed in the G1-S transition of cancer cells. NUB1 depletion causes G0/G1 phase arrest due to CUL1 and CUL2 ubiquitin E3 ligase-dependent pathways.
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Distasio, Andrew. "Novel Regulators of Neural Crest and Neural Progenitor Survival." University of Cincinnati / OhioLINK, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1593170783550813.

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Richet, E. "The modulation of tau aggregation in a cell model of Alzheimer's disease by the proteasome adaptor protein NUB1." Thesis, University College London (University of London), 2012. http://discovery.ucl.ac.uk/1355106/.

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Neurofibrillary tangles (NFT) in Alzheimer's disease (AD) are mainly composed of hyperphosphorylated and aggregated wild-type tau. NFTs are decorated by the ubiquitin-like modifier NEDD8, a protein targeted for proteasomal degradation by the NEDD8 Ultimate Buster 1 (NUB1). NUB1 has been shown to reduce synphilin-1 positive inclusions in a model of Parkinson’s disease. Therefore, this study examined the subcellular localisation of NUB1 as well as the effect of NUB1 on tau phosphorylation and aggregation. Furthermore, the effect of reducing NUB1 expression by RNA interference was investigated. Brain sections from AD patients showed that NUB1 and NEDD8 were expressed in the pyramidal neurons of the hippocampus, where the accumulation of NFTs is most abundant. In rat primary cortical neurons, NUB1 and tau co-localised in neurites and signalling structures such as varicosities, suggesting a functional interaction between them. The upregulation of the tau kinase GSK3β in AD leads to increased tau hyperphosphorylation and accumulation. In SK-N-SH neuroblastoma cells, which lack endogenous tau, ectopic wild-type tau formed inclusions when it was co-expressed with GSK3β, and this was enhanced by proteasome inhibition. NUB1 co-localised with both tau and GSK3β and significantly reduced tau inclusion formation. In neuroblastoma cells, NUB1 could interact with both tau and GSK3β, disrupt their interaction, and decrease the GSK3β-dependent phosphorylation of tau. NUB1 can directly bind synphilin-1 and induce its proteasomal degradation. Therefore, the ability of NUB1 to regulate GSK3β degradation was investigated in neuroblastoma cells. The upregulation of NUB1 accelerated the turnover of GSK3β, and the ubiquitin-associated (UBA) domains of NUB1 were necessary for NUB1 to exert its effect. Conversely, the downregulation of endogenous NUB1 by RNA interference increased the stability of endogenous GSK3β. Thus, NUB1 might have a role in tau inclusion formation by modulating GSK3β levels.
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Hildreth, Sherry Boston. "Investigation of Protein-Protein Interactions among Nicotine Biosynthetic Enzymes and Characterization of a Nicotine Transporter." Diss., Virginia Tech, 2003. http://hdl.handle.net/10919/29698.

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Alkaloids are a class of plant secondary metabolites produced in about 20% of plant families. Domesticated tobacco, Nicotiana tabacum produces nicotine as the predominant alkaloid. The biosynthesis of nicotine occurs exclusively in the roots of tobacco, yet accumulates in the leaves of tobacco where it is acts as a defense compound to deter insect herbivory. The research detailed in this dissertation addresses two aspects of nicotine physiology in tobacco: 1) an investigation of hypothesized protein-protein interactions among nicotine biosynthetic enzymes and 2) the characterization of a novel nicotine transporter. A hypothesized metabolic channel including the two nicotine biosynthetic enzymes putrescine N-methyltransferase (PMT), N-methylputrescine Oxidase (MPO) and the S-adenosylmethionine (SAM) recycling enzyme S-adenosylhomocysteine hydrolase (SAHH) has been proposed. To further explore this hypothesis, protein-protein interactions among nicotine biosynthetic enzymes PMT, MPO and SAHH were investigated using yeast two-hybrid assays and co-immunoprecipitation experiments. The yeast two-hybrid was conducted as both a directed screen to detect interactions between the hypothesized metabolic channel members and as a library screen to detect interactions between hypothesized metabolic channel members and proteins from a tobacco root cDNA library. Co-immunoprecipitation experiments were conducted using proteins produced in an in vitro transcription/ translation system and using native proteins from a tobacco root extract. The outcome of these experiments provided no further evidence of a nicotine metabolic channel and a discussion of the methods and outcomes of the experiments conducted is presented. The nicotine uptake permease, NUP1, was identified in tobacco roots and was shown to preferentially transport nicotine when expressed in Schizosaccharomyces pombe. This report presents the characterization of tobacco plants and hairy roots with diminished NUP1 transcripts created by using RNAi. The NUP1-RNAi hairy roots and plants showed a decreased level of nicotine and the hairy root cultures displayed an altered distribution of nicotine from the root to the culture medium. Additionally NUP1-GFP was used to determine that NUP1 localized to the plasma membrane of tobacco BY-2 protoplasts. Potential models for the role of NUP1 in nicotine physiology will be discussed.
Ph. D.
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Hildreth, Sherry B. "Investigation of Protein-Protein Interactions among Nicotine Biosynthetic Enzymes and Characterization of a Nicotine Transporter." Diss., Virginia Tech, 2009. http://hdl.handle.net/10919/29698.

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Alkaloids are a class of plant secondary metabolites produced in about 20% of plant families. Domesticated tobacco, Nicotiana tabacum produces nicotine as the predominant alkaloid. The biosynthesis of nicotine occurs exclusively in the roots of tobacco, yet accumulates in the leaves of tobacco where it is acts as a defense compound to deter insect herbivory. The research detailed in this dissertation addresses two aspects of nicotine physiology in tobacco: 1) an investigation of hypothesized protein-protein interactions among nicotine biosynthetic enzymes and 2) the characterization of a novel nicotine transporter. A hypothesized metabolic channel including the two nicotine biosynthetic enzymes putrescine N-methyltransferase (PMT), N-methylputrescine Oxidase (MPO) and the S-adenosylmethionine (SAM) recycling enzyme S-adenosylhomocysteine hydrolase (SAHH) has been proposed. To further explore this hypothesis, protein-protein interactions among nicotine biosynthetic enzymes PMT, MPO and SAHH were investigated using yeast two-hybrid assays and co-immunoprecipitation experiments. The yeast two-hybrid was conducted as both a directed screen to detect interactions between the hypothesized metabolic channel members and as a library screen to detect interactions between hypothesized metabolic channel members and proteins from a tobacco root cDNA library. Co-immunoprecipitation experiments were conducted using proteins produced in an in vitro transcription/ translation system and using native proteins from a tobacco root extract. The outcome of these experiments provided no further evidence of a nicotine metabolic channel and a discussion of the methods and outcomes of the experiments conducted is presented. The nicotine uptake permease, NUP1, was identified in tobacco roots and was shown to preferentially transport nicotine when expressed in Schizosaccharomyces pombe. This report presents the characterization of tobacco plants and hairy roots with diminished NUP1 transcripts created by using RNAi. The NUP1-RNAi hairy roots and plants showed a decreased level of nicotine and the hairy root cultures displayed an altered distribution of nicotine from the root to the culture medium. Additionally NUP1-GFP was used to determine that NUP1 localized to the plasma membrane of tobacco BY-2 protoplasts. Potential models for the role of NUP1 in nicotine physiology will be discussed.
Ph. D.
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Olsson, Magnus. "Nuclear pore membrane glycoprotein 210 as a new marker for epithelial cells." Doctoral thesis, Uppsala University, Department of Cell and Molecular Biology, 2003. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-3265.

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Epithelial cell polarisation is a prerequisite for the branching morphogenesis in several organs. Differential screening techniques were used to identify genes, which are upregulated during induction of epithelium in early kidney development. This investigation revealed two separate genes, Nuclear localising protein 1 (Nulp1), a previously undescribed gene with sequence characteristics of the basic helix-loop-helix transcription factor family, and glycoprotein 210 (gp210, POM210), an integral membrane protein constituent of the nuclear pore complex (NPC). Of these, gp210 was found to be upreglated during conversion of mesenchyme to epithelium.

The nuclear envelope, which demarcates the nuclear region in the eukaryotic cell, consists of an inner and an outer membrane that are fused at the locations for NPCs. These large macromolecular assemblages are tube like structures connecting the cytoplasmic and nuclear compartments of the cell. NPCs serve as the only conduits for exchange of molecular information between these cellular rooms. Electron microscopy techniques have revealed detailed information about the NPC architecture. A number of proteins (nucleoporins) have been characterised and embodied as components of the NPC structure. Active, energy dependent nucleocytoplasmic transport of RNAs and proteins is mediated by a group of soluble receptor proteins, collectively termed karyopherins.

Gp210 has been suggested to be important for nuclear pore formation. Nevertheless, our analyses showed a limited expression pattern of gp210, with its mRNA and protein largely confined to epithelial cells in the mouse embryo. Furthermore, in several cell lines, gp210 was undetectable. The expression pattern of gp210 was not synchronised with some other nucleoporins, indicating NPC heterogeneity. Characterisation of the structure of the human gp210 gene, including its promoter region, gave insight about possible cell-type specific gene regulatory mechanisms.

Regulation of molecular traffic between the nucleus and the cytoplasm leads to transcriptional control. Cell specific configuration of the NPC structure, due to diffential expression of gp210, could be involved in this control. Gp210 could be of importance for the development of epithelial cell polarisation.

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Camponeschi, Francesca, Sabine Annemarie Elisabeth Heider, Simone Ciofi-Baffoni, and Lucia Banci. "Characterization of pathways for the Fe-S protein biogenesis in the human cytoplasm." Doctoral thesis, 2020. http://hdl.handle.net/2158/1217050.

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Human cytosolic monothiolglutaredoxin-3 (GLRX3) is a protein essential for the maturation of cytosolic [4Fe−4S] proteins. We show here that dimeric cluster-bridged GLRX3 transfers its [2Fe−2S]2+ clusters to the human P-loop NTPase NUBP1, an essential early component of the cytosolic iron−sulfur assembly (CIA) machinery. Specifically, we observed that [2Fe−2S]2+ clusters are transferred from GLRX3 to monomeric apo NUBP1 and reductively coupled to form [4Fe−4S]2+ clusters on both N-terminal CX13CX2CX5C and C-terminal CPXC motifs of NUBP1 in the presence of glutathione that acts as a reductant. In this process, cluster binding to the C-terminal motif of NUBP1 promotes protein dimerization, while cluster binding to the N-terminal motif does not affect the quaternary structure of NUBP1. The cluster transfer/assembly process is not complete on both N- and C-terminal motifs and indeed requires a reductant stronger than GSH to increase its efficiency. We also showed that the [4Fe−4S]2+ cluster formed at the N-terminal motif of NUBP1 is tightly bound, while the [4Fe−4S]2+ cluster bound at the C-terminal motif is labile. Our findings provide the first evidence for GLRX3 acting as a [2Fe−2S] cluster chaperone in the early stage of the CIA machinery. Iron-sulfur (Fe-S) clusters are among the most versatile cofactors in biology. Although Fe-S clusters formation can be achieved spontaneously in vitro with inorganic iron and sulfur sources, the in vivo behaviour is more complex and requires the so-called Fe-S biogenesis machineries. In the cytosol, the biogenesis of Fe-S proteins is assisted by the cytosolic Fe-S protein assembly machinery, which comprises at least thirteen known proteins, among which there are human ORAOV1 and YAE1. A hetero-complex formed by the two latter proteins facilitates Fe-S cluster insertion in the human ABC protein ABCE1 within a chain of binding events that are still not well understood. In the present work, ORAOV1 and the YAE1-ORAOV1 complex were produced and their structural and cluster binding properties spectroscopically investigated. It resulted that both ORAOV1 and the YAE1-ORAOV1 complex are characterized by well-structured alpha-helical regions and by unstructured, flexible regions, and are both able to bind a [4Fe-4S]2+ cluster. Bioinformatics and site-directed mutagenesis studies indicated that ORAOV1, and not YAE1, is the protein involved in [4Fe-4S]2+ cluster binding in the hetero-complex. ORAOV1 has indeed a conserved cluster-binding motif able to coordinate a [4Fe-4S] cluster. Overall, our data suggested that the YAE1-ORAOV1 complex might actively participate in the Fe-S cluster insertion into ABCE1 thanks to the [4Fe-4S]2+ cluster binding properties of ORAOV1.
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Book chapters on the topic "NUBP1"

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David, Dezső, Lígia S. Almeida, Maristella Maggi, Carlos Araújo, Stefan Imreh, Giovanna Valentini, György Fekete, and Irén Haltrich. "Clinical Severity of PGK1 Deficiency Due To a Novel p.E120K Substitution Is Exacerbated by Co-inheritance of a Subclinical Translocation t(3;14)(q26.33;q12), Disrupting NUBPL Gene." In JIMD Reports, 55–65. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/8904_2015_427.

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"Instructions for Number Games with game boards (NuB1–NuB2)." In Paired Maths Handbook, 55. Routledge, 2013. http://dx.doi.org/10.4324/9781315068091-30.

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Conference papers on the topic "NUBP1"

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Tan, KL, F. Pezzella, A. Harris, and O. Acuto. "PO-479 NUB1 as a prognostic marker in breast cancer: a retrospective, integrated genomic, transcriptomic, and protein analysis." In Abstracts of the 25th Biennial Congress of the European Association for Cancer Research, Amsterdam, The Netherlands, 30 June – 3 July 2018. BMJ Publishing Group Ltd, 2018. http://dx.doi.org/10.1136/esmoopen-2018-eacr25.982.

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