Počet záznamů: 1

Trypanosoma brucei Mitochondrial Respiratome: Composition and Organization in Procyclic Form

  1. 1.
    0367704 - BC-A 2012 RIV US eng J - Článek v odborném periodiku
    Acestor, N. - Zíková, Alena - Dalley, R. A. - Anupama, A. - Panigrahi, A. K. - Stuart, K. D.
    Trypanosoma brucei Mitochondrial Respiratome: Composition and Organization in Procyclic Form.
    Molecular and Cellular Proteomics. Roč. 10, č. 9 (2011), s. 1-14 ISSN 1535-9476
    Grant CEP: GA ČR GP204/09/P563
    Výzkumný záměr: CEZ:AV0Z60220518
    Klíčová slova: SUCCINATE DEHYDROGENASE * EDITED MESSENGER-RNA * COMPLEX-I * TRYPANOSOMA-BRUCEI * UBIQUINONE OXIDOREDUCTASE * TAP-TAG * PROTEIN INTERACTION * ALTERNATIVE OXIDASE * STATISTICAL-MODEL * MASS-SPECTROMETRY
    Kód oboru RIV: EB - Genetika a molekulární biologie
    Impakt faktor: 7.398, rok: 2011

    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. 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 showed that the respiratome of Trypanosoma is divergent because many of its proteins are unique to this group of organisms. 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.
    Trvalý link: http://hdl.handle.net/11104/0202286