دورية أكاديمية
أعرض في EDS

Branched late-steps of the cytosolic iron-sulphur cluster assembly machinery of Trypanosoma brucei.

التفاصيل البيبلوغرافية
العنوان: Branched late-steps of the cytosolic iron-sulphur cluster assembly machinery of Trypanosoma brucei.
المؤلفون: Tonini ML; Biomedical Sciences Research Complex (BSRC), University of St Andrews, St Andrews, Fife, United Kingdom., Peña-Diaz P; Biology Centre, Institute of Parasitology, Czech Academy of Sciences, České Budějovice (Budweis), Czech Republic., Haindrich AC; Biology Centre, Institute of Parasitology, Czech Academy of Sciences, České Budějovice (Budweis), Czech Republic.; Faculty of Sciences, University of South Bohemia, České Budějovice (Budweis), Czech Republic., Basu S; Biology Centre, Institute of Parasitology, Czech Academy of Sciences, České Budějovice (Budweis), Czech Republic.; Institut für Zytobiologie, Philipps-Universität Marburg, Marburg, Germany., Kriegová E; Biology Centre, Institute of Parasitology, Czech Academy of Sciences, České Budějovice (Budweis), Czech Republic., Pierik AJ; Faculty of Chemistry-Biochemistry, University of Kaiserslautern, Kaiserslautern, Germany., Lill R; Institut für Zytobiologie, Philipps-Universität Marburg, Marburg, Germany.; LOEWE Zentrum für synthetische Mikrobiologie, Marburg, Germany., MacNeill SA; Biomedical Sciences Research Complex (BSRC), University of St Andrews, St Andrews, Fife, United Kingdom., Smith TK; Biomedical Sciences Research Complex (BSRC), University of St Andrews, St Andrews, Fife, United Kingdom., Lukeš J; Biology Centre, Institute of Parasitology, Czech Academy of Sciences, České Budějovice (Budweis), Czech Republic.; Faculty of Sciences, University of South Bohemia, České Budějovice (Budweis), Czech Republic.
المصدر: PLoS pathogens [PLoS Pathog] 2018 Oct 22; Vol. 14 (10), pp. e1007326. Date of Electronic Publication: 2018 Oct 22 (Print Publication: 2018).
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Public Library of Science Country of Publication: United States NLM ID: 101238921 Publication Model: eCollection Cited Medium: Internet ISSN: 1553-7374 (Electronic) Linking ISSN: 15537366 NLM ISO Abbreviation: PLoS Pathog Subsets: MEDLINE
أسماء مطبوعة: Original Publication: San Francisco, CA : Public Library of Science, c2005-
مواضيع طبية MeSH: Cytosol/*metabolism , Iron-Sulfur Proteins/*metabolism , Protozoan Proteins/*metabolism , Trypanosoma brucei brucei/*metabolism , Trypanosomiasis/*parasitology, Animals ; Female ; Iron-Sulfur Proteins/chemistry ; Mice ; Mice, Inbred BALB C ; Protein Conformation ; Protein Interaction Domains and Motifs ; Protozoan Proteins/chemistry ; Trypanosoma brucei brucei/growth & development ; Trypanosomiasis/metabolism
مستخلص: Fe-S clusters are ubiquitous cofactors of proteins involved in a variety of essential cellular processes. The biogenesis of Fe-S clusters in the cytosol and their insertion into proteins is accomplished through the cytosolic iron-sulphur protein assembly (CIA) machinery. The early- and middle-acting modules of the CIA pathway concerned with the assembly and trafficking of Fe-S clusters have been previously characterised in the parasitic protist Trypanosoma brucei. In this study, we applied proteomic and genetic approaches to gain insights into the network of protein-protein interactions of the late-acting CIA targeting complex in T. brucei. All components of the canonical CIA machinery are present in T. brucei including, as in humans, two distinct CIA2 homologues TbCIA2A and TbCIA2B. These two proteins are found interacting with TbCIA1, yet the interaction is mutually exclusive, as determined by mass spectrometry. Ablation of most of the components of the CIA targeting complex by RNAi led to impaired cell growth in vitro, with the exception of TbCIA2A in procyclic form (PCF) trypanosomes. Depletion of the CIA-targeting complex was accompanied by reduced levels of protein-bound cytosolic iron and decreased activity of an Fe-S dependent enzyme in PCF trypanosomes. We demonstrate that the C-terminal domain of TbMMS19 acts as a docking site for TbCIA2B and TbCIA1, forming a trimeric complex that also interacts with target Fe-S apo-proteins and the middle-acting CIA component TbNAR1.
Competing Interests: The authors have declared that no competing interests exist.
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المشرفين على المادة: 0 (Iron-Sulfur Proteins)
0 (Protozoan Proteins)
تواريخ الأحداث: Date Created: 20181023 Date Completed: 20190306 Latest Revision: 20190306
رمز التحديث: 20231215
مُعرف محوري في PubMed: PMC6211773
DOI: 10.1371/journal.ppat.1007326
PMID: 30346997
قاعدة البيانات: MEDLINE
الوصف
تدمد:1553-7374
DOI:10.1371/journal.ppat.1007326