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Cytosolic iron‐sulphur protein assembly is functionally conserved and essential in procyclic and bloodstream T rypanosoma brucei
Author(s) -
Basu Somsuvro,
Netz Daili J.,
Haindrich Alexander C.,
Herlerth Nils,
Lagny Thibaut J.,
Pierik Antonio J.,
Lill Roland,
Lukeš Julius
Publication year - 2014
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.12706
Subject(s) - biology , cytosol , trypanosoma brucei , aconitase , microbiology and biotechnology , saccharomyces cerevisiae , biochemistry , biogenesis , protein targeting , yeast , mitochondrion , membrane protein , gene , enzyme , membrane
Summary 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 T rypanosoma 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 T ah18 was characterized as a flavoprotein, while its binding partner D re2 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 E xcavata.