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Protein composition of Trypanosoma brucei mitochondrial membranes
Author(s) -
Acestor Nathalie,
Panigrahi Aswini K.,
Ogata Yuko,
Anupama Atashi,
Stuart Kenneth D.
Publication year - 2009
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200900354
Subject(s) - trypanosoma brucei , intermembrane space , inner membrane , biology , translocase of the inner membrane , mitochondrial carrier , membrane protein , mitochondrion , transmembrane protein , biochemistry , membrane , translocase of the outer membrane , cell fractionation , protein targeting , inner mitochondrial membrane , transmembrane domain , microbiology and biotechnology , mitochondrial membrane transport protein , bacterial outer membrane , gene , escherichia coli , receptor
Mitochondria consist of four compartments, outer membrane, intermembrane space, inner membrane, and matrix; each harboring specific functions and structures. In this study, we used LC‐MS/MS to characterize the protein composition of Trypanosoma brucei mitochondrial (mt) membranes, which were enriched by different biochemical fractionation techniques. The analyses identified 202 proteins that contain one or more transmembrane domain(s) and/or positive GRAVY scores. Of these, various criteria were used to assign 72 proteins to mt membranes with high confidence, and 106 with moderate‐to‐low confidence. The sub‐cellular localization of a selected subset of 13 membrane assigned proteins was confirmed by tagging and immunofluorescence analysis. While most proteins assigned to mt membrane have putative roles in metabolic, energy generating, and transport processes, ∼50% have no known function. These studies result in a comprehensive profile of the composition and sub‐organellar location of proteins in the T. brucei mitochondrion thus, providing useful information on mt functions.