Trypanosoma brucei mitochondrial respiratome: Composition and organization in procyclic form
Dalley, Rachel A.
Panigrahi, Aswini Kumar
Stuart, Kenneth D.
Online Publication Date2011-05-24
Print Publication Date2011-09
Permanent link to this recordhttp://hdl.handle.net/10754/561781
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AbstractThe mitochondrial respiratory chain is comprised of four different protein complexes (I-IV), which are responsible for electron transport and generation of proton gradient in the mitochondrial intermembrane space. This proton gradient is then used by F oF 1-ATP synthase (complex V) to produce ATP by oxidative phosphorylation. In this study, the respiratory complexes I, II, and III were affinity purified from Trypanosoma brucei procyclic form cells and their composition was determined by mass spectrometry. The results along with those that we previously reported for complexes IV and V showed that the respiratome of Trypanosoma is divergent because many of its proteins are unique to this group of organisms. The studies also identified two mitochondrial subunit proteins of respiratory complex IV that are encoded by edited RNAs. Proteomics data from analyses of complexes purified using numerous tagged component proteins in each of the five complexes were used to generate the first predicted protein-protein interaction network of the Trypanosoma brucei respiratory chain. These results provide the first comprehensive insight into the unique composition of the respiratory complexes in Trypanosoma brucei, an early diverged eukaryotic pathogen. © 2011 by The American Society for Biochemistry and Molecular Biology, Inc.
CitationAcestor, N., Zíková, A., Dalley, R. A., Anupama, A., Panigrahi, A. K., & Stuart, K. D. (2011). Trypanosoma bruceiMitochondrial Respiratome: Composition and Organization in Procyclic Form. Molecular & Cellular Proteomics, 10(9), M110.006908. doi:10.1074/mcp.m110.006908
SponsorsThis work was supported by National Institutes of Health grant AI065935 to KS. AZ received support from grant 204/09/P563 from the Grant Agency of the Czech Republic. Research was conducted using equipment made possible by support from the Economic Development Administration - US Department of Commerce and the M.J. Murdock Charitable Trust.
JournalMolecular & Cellular Proteomics
PubMed Central IDPMC3186196
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