دورية أكاديمية
Cytosolic iron-sulphur protein assembly is functionally conserved and essential in procyclic and bloodstream Trypanosoma brucei.
العنوان: | Cytosolic iron-sulphur protein assembly is functionally conserved and essential in procyclic and bloodstream Trypanosoma brucei. |
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المؤلفون: | Basu S; Biology Centre, Institute of Parasitology, 37005, České Budějovice (Budweis), Czech Republic; Faculty of Sciences, University of South Bohemia, 37005, České Budějovice (Budweis), Czech Republic., Netz DJ, Haindrich AC, Herlerth N, Lagny TJ, Pierik AJ, Lill R, Lukeš J |
المصدر: | Molecular microbiology [Mol Microbiol] 2014 Sep; Vol. 93 (5), pp. 897-910. Date of Electronic Publication: 2014 Jul 23. |
نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
اللغة: | English |
بيانات الدورية: | Publisher: Blackwell Scientific Publications Country of Publication: England NLM ID: 8712028 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1365-2958 (Electronic) Linking ISSN: 0950382X NLM ISO Abbreviation: Mol Microbiol Subsets: MEDLINE |
أسماء مطبوعة: | Original Publication: Oxford, OX ; Boston, MA : Blackwell Scientific Publications, c1987- |
مواضيع طبية MeSH: | Cytosol/*metabolism , Iron-Sulfur Proteins/*metabolism , Protozoan Proteins/*metabolism , Trypanosoma brucei brucei/*growth & development , Trypanosoma brucei brucei/*metabolism , Trypanosomiasis, African/*parasitology, Amino Acid Sequence ; Humans ; Iron-Sulfur Proteins/chemistry ; Iron-Sulfur Proteins/genetics ; Molecular Sequence Data ; Protein Structure, Tertiary ; Protozoan Proteins/chemistry ; Protozoan Proteins/genetics ; Sequence Alignment ; Trypanosoma brucei brucei/chemistry ; Trypanosoma brucei brucei/genetics |
مستخلص: | Cytosolic and nuclear iron-sulphur (Fe/S) proteins include essential components involved in protein translation, DNA synthesis and DNA repair. In yeast and human cells, assembly of their Fe/S cofactor is accomplished by the CIA (cytosolic iron-sulphur protein assembly) machinery comprised of some 10 proteins. To investigate the extent of conservation of the CIA pathway, we examined its importance in the early-branching eukaryote Trypanosoma brucei that encodes all known CIA factors. Upon RNAi-mediated ablation of individual, early-acting CIA proteins, no major defects were observed in both procyclic and bloodstream stages. In contrast, parallel depletion of two CIA components was lethal, and severely diminished cytosolic aconitase activity lending support for a direct role of the CIA proteins in cytosolic Fe/S protein biogenesis. In support of this conclusion, the T. brucei CIA proteins complemented the growth defects of their respective yeast CIA depletion mutants. Finally, the T. brucei CIA factor Tah18 was characterized as a flavoprotein, while its binding partner Dre2 functions as a Fe/S protein. Together, our results demonstrate the essential and conserved function of the CIA pathway in cytosolic Fe/S protein assembly in both developmental stages of this representative of supergroup Excavata. (© 2014 John Wiley & Sons Ltd.) |
المشرفين على المادة: | 0 (Iron-Sulfur Proteins) 0 (Protozoan Proteins) |
تواريخ الأحداث: | Date Created: 20140722 Date Completed: 20150511 Latest Revision: 20140901 |
رمز التحديث: | 20240628 |
DOI: | 10.1111/mmi.12706 |
PMID: | 25040552 |
قاعدة البيانات: | MEDLINE |
تدمد: | 1365-2958 |
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DOI: | 10.1111/mmi.12706 |