Trypanosoma brucei mitochondrial respiratome: Composition and organization in procyclic form

Handle URI:
http://hdl.handle.net/10754/561781
Title:
Trypanosoma brucei mitochondrial respiratome: Composition and organization in procyclic form
Authors:
Acestor, Nathalie; Zíková, Alena; Dalley, Rachel A.; Anupama, Atashi; Panigrahi, Aswini Kumar; Stuart, Kenneth D.
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.
KAUST Department:
Core Labs
Publisher:
American Society for Biochemistry & Molecular Biology (ASBMB)
Journal:
Molecular & Cellular Proteomics
Issue Date:
24-May-2011
DOI:
10.1074/mcp.M110.006908
PubMed ID:
21610103
PubMed Central ID:
PMC3186196
Type:
Article
ISSN:
15359476
Sponsors:
This 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.
Additional Links:
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3186196
Appears in Collections:
Articles

Full metadata record

DC FieldValue Language
dc.contributor.authorAcestor, Nathalieen
dc.contributor.authorZíková, Alenaen
dc.contributor.authorDalley, Rachel A.en
dc.contributor.authorAnupama, Atashien
dc.contributor.authorPanigrahi, Aswini Kumaren
dc.contributor.authorStuart, Kenneth D.en
dc.date.accessioned2015-08-03T09:04:28Zen
dc.date.available2015-08-03T09:04:28Zen
dc.date.issued2011-05-24en
dc.identifier.issn15359476en
dc.identifier.pmid21610103en
dc.identifier.doi10.1074/mcp.M110.006908en
dc.identifier.urihttp://hdl.handle.net/10754/561781en
dc.description.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.en
dc.description.sponsorshipThis 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.en
dc.publisherAmerican Society for Biochemistry & Molecular Biology (ASBMB)en
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3186196en
dc.titleTrypanosoma brucei mitochondrial respiratome: Composition and organization in procyclic formen
dc.typeArticleen
dc.contributor.departmentCore Labsen
dc.identifier.journalMolecular & Cellular Proteomicsen
dc.identifier.pmcidPMC3186196en
dc.contributor.institutionSeattle Biomedical Research Institute, 307 Westlake Ave N, Seattle, WA 98109-5219, United Statesen
dc.contributor.institutionBiology Center, Institute of Parasitology, University of South Bohemia, České Budějovice, Czech Republicen
kaust.authorPanigrahi, Aswini Kumaren

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