Trypanosoma brucei mitochondrial respiratome: Composition and organization in procyclic form

Nathalie Acestor, Alena Zíková, Rachel A. Dalley, Atashi Anupama, Aswini Kumar Panigrahi, Kenneth D. Stuart

Research output: Contribution to journalArticlepeer-review

48 Scopus citations

Abstract

The 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.
Original languageEnglish (US)
Pages (from-to)M110.006908
JournalMolecular & Cellular Proteomics
Volume10
Issue number9
DOIs
StatePublished - May 24 2011

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Analytical Chemistry

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