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Relevant bibliographies by topics / [Fe-S] protein

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Academic literature on the topic '[Fe-S] protein'

Author: Grafiati

Published: 4 June 2021

Last updated: 13 February 2022

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Journal articles on the topic "[Fe-S] protein"

1

Zhang, Yan, Elise R. Lyver, Eiko Nakamaru-Ogiso, et al. "Dre2, a Conserved Eukaryotic Fe/S Cluster Protein, Functions in Cytosolic Fe/S Protein Biogenesis." Molecular and Cellular Biology 28, no. 18 (2008): 5569–82. http://dx.doi.org/10.1128/mcb.00642-08.

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ABSTRACT In a forward genetic screen for interaction with mitochondrial iron carrier proteins in Saccharomyces cerevisiae, a hypomorphic mutation of the essential DRE2 gene was found to confer lethality when combined with Δmrs3 and Δmrs4. The dre2 mutant or Dre2-depleted cells were deficient in cytosolic Fe/S cluster protein activities while maintaining mitochondrial Fe/S clusters. The Dre2 amino acid sequence was evolutionarily conserved, and cysteine motifs (CX2CXC and twin CX2C) in human and yeast proteins were perfectly aligned. The human Dre2 homolog (implicated in blocking apoptosis and

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Dos Santos, Patricia C., and Dennis R. Dean. "Electrons in Fe-S protein assembly." Nature Chemical Biology 6, no. 10 (2010): 700–701. http://dx.doi.org/10.1038/nchembio.438.

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Paul, Viktoria Désirée, and Roland Lill. "SnapShot: Eukaryotic Fe-S Protein Biogenesis." Cell Metabolism 20, no. 2 (2014): 384–384. http://dx.doi.org/10.1016/j.cmet.2014.07.010.

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Balk, J., A. J. Pierik, D. J. Aguilar Netz, U. Mühlenhoff, and R. Lill. "Nar1p, a conserved eukaryotic protein with similarity to Fe-only hydrogenases, functions in cytosolic iron-sulphur protein biogenesis." Biochemical Society Transactions 33, no. 1 (2005): 86–89. http://dx.doi.org/10.1042/bst0330086.

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The genome of the yeast Saccharomyces cerevisiae encodes the essential protein Nar1p that is conserved in virtually all eukaryotes and exhibits striking sequence similarity to bacterial iron-only hydrogenases. Previously, we have shown that Nar1p is an Fe-S protein and that assembly of its co-factors depends on the mitochondrial Fe-S cluster biosynthesis apparatus. Using functional studies in vivo, we demonstrated that Nar1p has an essential role in the maturation of cytosolic and nuclear, but not of mitochondrial, Fe-S proteins [Balk, Pierik, Aguilar Netz, Mühlenhoff and Lill (2004) EMBO J. 2

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Gerber, Jana, Karina Neumann, Corinna Prohl, Ulrich Mühlenhoff, and Roland Lill. "The Yeast Scaffold Proteins Isu1p and Isu2p Are Required inside Mitochondria for Maturation of Cytosolic Fe/S Proteins." Molecular and Cellular Biology 24, no. 11 (2004): 4848–57. http://dx.doi.org/10.1128/mcb.24.11.4848-4857.2004.

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ABSTRACT Iron-sulfur (Fe/S) proteins are located in mitochondria, cytosol, and nucleus. Mitochondrial Fe/S proteins are matured by the iron-sulfur cluster (ISC) assembly machinery. Little is known about the formation of Fe/S proteins in the cytosol and nucleus. A function of mitochondria in cytosolic Fe/S protein maturation has been noted, but small amounts of some ISC components have been detected outside mitochondria. Here, we studied the highly conserved yeast proteins Isu1p and Isu2p, which provide a scaffold for Fe/S cluster synthesis. We asked whether the Isu proteins are needed for bios

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Balk, Janneke, Daili J. Aguilar Netz, Katharina Tepper, Antonio J. Pierik, and Roland Lill. "The Essential WD40 Protein Cia1 Is Involved in a Late Step of Cytosolic and Nuclear Iron-Sulfur Protein Assembly." Molecular and Cellular Biology 25, no. 24 (2005): 10833–41. http://dx.doi.org/10.1128/mcb.25.24.10833-10841.2005.

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ABSTRACT The assembly of cytosolic and nuclear iron-sulfur (Fe/S) proteins in yeast is dependent on the iron-sulfur cluster assembly and export machineries in mitochondria and three recently identified extramitochondrial proteins, the P-loop NTPases Cfd1 and Nbp35 and the hydrogenase-like Nar1. However, the molecular mechanism of Fe/S protein assembly in the cytosol is far from being understood, and more components are anticipated to take part in this process. Here, we have identified and functionally characterized a novel WD40 repeat protein, designated Cia1, as an essential component require

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Stehling, Oliver, Daili J. A. Netz, Brigitte Niggemeyer, et al. "Human Nbp35 Is Essential for both Cytosolic Iron-Sulfur Protein Assembly and Iron Homeostasis." Molecular and Cellular Biology 28, no. 17 (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 asso

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Gomez-Casati, Diego F., Maria V. Busi, Julieta Barchiesi, Maria A. Pagani, Noelia S. Marchetti-Acosta, and Agustina Terenzi. "Fe-S Protein Synthesis in Green Algae Mitochondria." Plants 10, no. 2 (2021): 200. http://dx.doi.org/10.3390/plants10020200.

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Iron and sulfur are two essential elements for all organisms. These elements form the Fe-S clusters that are present as cofactors in numerous proteins and protein complexes related to key processes in cells, such as respiration and photosynthesis, and participate in numerous enzymatic reactions. In photosynthetic organisms, the ISC and SUF Fe-S cluster synthesis pathways are located in organelles, mitochondria, and chloroplasts, respectively. There is also a third biosynthetic machinery in the cytosol (CIA) that is dependent on the mitochondria for its function. The genes and proteins that par

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Lill, Roland. "From the discovery to molecular understanding of cellular iron-sulfur protein biogenesis." Biological Chemistry 401, no. 6-7 (2020): 855–76. http://dx.doi.org/10.1515/hsz-2020-0117.

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AbstractProtein cofactors often are the business ends of proteins, and are either synthesized inside cells or are taken up from the nutrition. A cofactor that strictly needs to be synthesized by cells is the iron-sulfur (Fe/S) cluster. This evolutionary ancient compound performs numerous biochemical functions including electron transfer, catalysis, sulfur mobilization, regulation and protein stabilization. Since the discovery of eukaryotic Fe/S protein biogenesis two decades ago, more than 30 biogenesis factors have been identified in mitochondria and cytosol. They support the synthesis, traff

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Frazzon, J., J. R. Fick, and D. R. Dean. "Biosynthesis of iron-sulphur clusters is a complex and highly conserved process." Biochemical Society Transactions 30, no. 4 (2002): 680–85. http://dx.doi.org/10.1042/bst0300680.

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Iron-sulphur ([Fe-S]) clusters are simple inorganic prosthetic groups that are contained in a variety of proteins having functions related to electron transfer, gene regulation, environmental sensing and substrate activation. In spite of their simple structures, biological [Fe-S] clusters are not formed spontaneously. Rather, a consortium of highly conserved proteins is required for both the formation of [Fe-S] clusters and their insertion into various protein partners. Among the [Fe-S] cluster biosynthetic proteins are included a pyridoxal phosphate-dependent enzyme (NifS) that is involved in

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Dissertations / Theses on the topic "[Fe-S] protein"

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Christ, Stefan [Verfasser], and Ulrich [Akademischer Betreuer] Mühlenhoff. "Analyse von posttranslationalen Modifikationen an Fe/S-Proteinen und Protein-Protein-Interaktionen zwischen Fe/S-Assemblierungsfaktoren in Mitochondrien von S. cerevisiae / Stefan Christ. Betreuer: Ulrich Mühlenhoff." Marburg : Philipps-Universität Marburg, 2016. http://d-nb.info/1099594308/34.

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Molik, Sabine. "Das plastidäre Rieske Fe/S-Protein Analyse des Transport- und Assemblierungsprozesses /." [S.l. : s.n.], 2005. http://deposit.ddb.de/cgi-bin/dokserv?idn=975694057.

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Salter, A. Hugh. "Genetics and biogensis of the pea chloroplast Rieske Fe-S protein." Thesis, University of Cambridge, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.335798.

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Jayawardhana, W. Geethamala Dhananjalee. "Investigation of the Influence of Transition Metal Ions on the Fe-S Cluster Biosynthesis Protein SufU." Bowling Green State University / OhioLINK, 2015. http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1448034834.

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Salameh, Myriam. "CISD2, protéine à centre Fe-S impliquée dans différentes pathologies humaines New Insights of the NEET Protein CISD2 Reveals Distinct Features Compared to Its Close Mitochondrial Homolog mitoNEET." Thesis, université Paris-Saclay, 2021. http://www.theses.fr/2021UPASL025.

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CISD2 appartient à la famille de protéines NEET caractérisée par une coordination atypique de leur centre [2Fe-2S] par trois cystéines et une histidine, et leur capacité à transférer leur centre [Fe-S] in vitro vers une protéine acceptrice. CISD2 est une protéine homodimérique ancrée au niveau des sites de contact entre le réticulum endoplasmique et la mitochondrie avec un centre [2Fe-2S] par protomère. La majeure partie de CISD2, dont son domaine de coordination du centre [Fe-S], est cytosolique. Ce dernier est très proche en séquence et en structure de celui de mitoNEET, autre membre de la f

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Mons, Cécile. "Etude biochimique de mitoNEET humaine, protéine à centre [2Fe-2S], impliquée dans une voie de réparation des protéines Fe-S suite à un stress oxydatif." Thesis, Université Paris-Saclay (ComUE), 2017. http://www.theses.fr/2017SACLS409.

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Présente chez les mammifères, mitoNEET (mNT) est une protéine à centre Fe-S ancrée à la membrane externe de la mitochondrie. Cette protéine dimérique possède un centre [2Fe-2S] par monomère lié de façon atypique à la protéine par trois cystéines et une histidine. Notre équipe a auparavant montré l’implication de mNT dans une nouvelle voie de réparation du centre [4Fe-4S] de l’Iron Regulatory Protein-1 (IRP-1), régulateur majeur de l’homéostasie du fer intracellulaire, par transfert du centre Fe-S de mNT à l’IRP-1 à réparer. Au cours de ma thèse, je me suis focalisée sur la caractérisation in v

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Leipuviene, Ramune. "Frameshifting as a tool in analysis of transfer RNA modification and translation." Doctoral thesis, Umeå universitet, Molekylärbiologi (Teknat- och Medfak), 2004. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-302.

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Studies of ribosomal reading frame maintenance are often based on frameshift mutation suppression experiments. In this thesis, suppression of a frameshift mutation in Salmonella enterica serovar Typhimurium by a tRNA and a ribosomal protein are described. The +1 frameshift mutation hisC3072 (that contains an extra G in a run of Gs) is corrected by mutations in the argU gene coding for the minor tRNAArgmnm5UCU. The altered tRNAArgmnm5UCU has a decreased stability and reduced aminoacylation due to changed secondary and/or tertiary structure. Protein sequencing revealed that during the translatio

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Reinhard, Annegret S. [Verfasser]. "Mössbauer-Spektroskopie- und Dichte-Funktional-Theorie-Untersuchungen an Modellkomplexen der [Fe]-Hydrogenase und dem Protein LytB / Annegret S. Reinhard." Aachen : Shaker, 2012. http://d-nb.info/1051576075/34.

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Amela, Abellan Isaac. "Bioinformatics Approaches to Protein Interaction and Complexes: Application to Pathogen-Host Epitope Mimicry and to Fe-S Cluster Biogenesis Model." Doctoral thesis, Universitat Autònoma de Barcelona, 2013. http://hdl.handle.net/10803/125908.

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Les interaccions antigen/anticòs són un dels tipus més interessants d’interaccions proteiques. La millor manera de prevenir les malalties causades per patògens és mitjançant l’ús de vacunes. L’aparició de la genòmica permet fer cerques a tot el genoma de nous candidats vacunals, tècnica anomenada vaccinologia inversa. L’estratègia més comuna on s’aplica la vaccinologia inversa és al disseny de vacunes de subunitats recombinants, que en general generen resposta immune humoral a causa de la presència d’epítops B en les proteïnes del patogen. Un problema important d’aquesta estratègia és la ident

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Bian, Shumin. "Fe-S proteins : cluster assembly and degradation /." The Ohio State University, 1998. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487952208109007.

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Books on the topic "[Fe-S] protein"

1

Dos Santos, Patricia C., ed. Fe-S Proteins. Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1605-5.

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David, Sheila S. Fe-S Cluster Enzymes. Elsevier Science & Technology Books, 2017.

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Fe-S Cluster Enzymes Part B, Volume 599. Academic Press, 2018.

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Book chapters on the topic "[Fe-S] protein"

1

Carter, Terrell D., and F. Wayne Outten. "Ni-NTA Affinity Chromatography to Characterize Protein–Protein Interactions During Fe-S Cluster Biogenesis." In Methods in Molecular Biology. Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1605-5_7.

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Kesawat, Mahipal Singh, Basanta Kumar Das, Manu Kumar, Govindaraj Ramakantrao Bhaganagare, and Manorama. "An Overview on Fe-S Protein Biogenesis from Prokaryotes to Eukaryotes." In Biological Nitrogen Fixation. John Wiley & Sons, Inc, 2015. http://dx.doi.org/10.1002/9781119053095.ch6.

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Salter, A. Hugh, Barbara J. Newman, and John C. Gray. "Characterization of cDNA Clones Encoding the Pea Chloroplast Rieske Fe-S Protein." In Techniques and New Developments in Photosynthesis Research. Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-8571-4_54.

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Darrouzet, Elisabeth, Maria Valkova-Valchanova, and Fevzi Daldal. "Role of the Neck Region of the Rieske Fe-S Protein in Qo Site Catalysis." In Photosynthesis: Mechanisms and Effects. Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-3953-3_356.

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Gubernator, Beata, Udo Johanningmeier, and Andrzej Szczepaniak. "Overproduction of a Spinach Rieske Fe-S Polypeptide Fused to Maltose-binding Protein in Escherichia coli." In Photosynthesis: Mechanisms and Effects. Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-3953-3_365.

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Salter, A. Hugh, and John C. Gray. "Characterisation of a Full-Length cDNA Clone Encoding the Pea Rieske Fe-S Protein : Import and Processing by Isolated Chloroplasts." In Current Research in Photosynthesis. Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0511-5_496.

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Charan, Manish, and Saman Habib. "Biosynthesis of Fe+-S Proteins and Their Roles." In Encyclopedia of Malaria. Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4614-8757-9_44-2.

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Ueda, Chie, Michelle Langton, and Maria-Eirini Pandelia. "Characterization of Fe-S Clusters in Proteins by." In Methods in Molecular Biology. Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1605-5_15.

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Corless, Elliot I., and Edwin Antony. "Methods for Heterologous Overproduction of Fe-S Proteins." In Methods in Molecular Biology. Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1605-5_4.

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Cramer, Stephen P., Yuming Xiao, Hongxin Wang, Yisong Guo, and Matt C. Smith. "Nuclear Resonance Vibrational Spectroscopy (NRVS) of Fe-S model compounds, Fe-S proteins, and nitrogenase." In NASSAU 2006. Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-71127-8_5.

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Conference papers on the topic "[Fe-S] protein"

1

Torrens, Francisco, and Gloria Castellano. "Calculation of partition coefficients of Fe–S/Se protein models." In The 11th International Electronic Conference on Synthetic Organic Chemistry. MDPI, 2007. http://dx.doi.org/10.3390/ecsoc-11-01365.

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Rafikova, O., M. Niihori, C. A. Eccles, M. Vasilyev, and R. Rafikov. "Pulmonary Hypertension and Metabolic Disease in Rats with Human Mutation in Fe-S Cluster Scaffold Protein NFU1." 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.a5870.

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RUZAIĶE, Aija, Sandra MUIŽNIECE-BRASAVA, Zanda KRŪMA, and Kaspars KOVAĻENKO. "NUTRITIONAL VALUE DETERMINATION OF THERMALLY PROCESSED POTATO MAIN COURSE IN RETORT PACKAGING." In RURAL DEVELOPMENT. Aleksandras Stulginskis University, 2018. http://dx.doi.org/10.15544/rd.2017.078.

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Consumers are increasingly demanding choices of ready-made foods with excellent organoleptic and health-related properties. There are two main trends in Europe; firstly, consumers are increasingly choosing foods that are comfortable for use, secondly, the number of people who are overweight is increasing, with more consumers paying close attention to the ingredients and nutritional value of products in order to balance the amount of the food they consume per day. The aim of the research was to develop new potato main courses and to determine their nutritional value. The research was carried ou

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Farmer, J. C., J. J. Haslam, S. D. Day, et al. "Corrosion Resistance of Iron-Based Amorphous Metal Coatings." In ASME 2006 Pressure Vessels and Piping/ICPVT-11 Conference. ASMEDC, 2006. http://dx.doi.org/10.1115/pvp2006-icpvt-11-93835.

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New amorphous-metal thermal-spray coatings have been developed recently that may provide a viable coating option for spent nuclear fuel & high-level waste repositories [Pang et al. 2002; Shinimiya et al. 2005; Ponnambalam et al. 2004; Branagan et al. 2000–2004]. Some Fe-based amorphous-metal formulations have been found to have corrosion resistance comparable to that of high-performance alloys such as Ni-based Alloy C-22 [Farmer et al. 2004–2006]. These materials rely on Cr, Mo and W for enhanced corrosion resistance, while B is added to promote glass formation and Y is added to lower the

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