Mass spectrometric analysis of the editosome and other multiprotein complexes in Trypanosoma brucei.
The composition of the editosome, a multi-protein complex that catalyzes uridine insertion and deletion RNA editing to produce mature mitochondrial mRNAs in trypanosomes, was analyzed by mass spectrometry. The editosomes were isolated by column chromatography, glycerol gradient sedimentation, and monoclonal antibody affinity purifications. At least 16 proteins form the catalytic core of the editosome, and additional associated proteins were identified. Analyses of mitochondrial fractions identified several non-editosome proteins and multi-protein complexes. These studies contribute to the functional annotation of T. brucei genome.
Panigrahi
Aswini K
AK
Department of Pathobiology, University of Washington, and Seattle Biomedical Research Institute, Seattle, Washington 98109, USA.
Allen
Thomas E
TE
Stuart
Kenneth
K
Haynes
Paul A
PA
Gygi
Steven P
SP
D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D046911:Macromolecular Substances; D013058:Mass Spectrometry; D008928:Mitochondria / Q000737:chemistry / Q000378:metabolism; D024101:Mitochondrial Proteins / Q000032:analysis / Q000737:chemistry / Q000378:metabolism; D008969:Molecular Sequence Data; D046912:Multiprotein Complexes; D021382:Protein Sorting Signals; D021381:Protein Transport; D015800:Protozoan Proteins / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism; D017393:RNA Editing; D016601:RNA-Binding Proteins / Q000032:analysis / Q000737:chemistry / Q000378:metabolism; D014346:Trypanosoma brucei brucei / Q000737:chemistry*
D046911:Macromolecular Substances; D024101:Mitochondrial Proteins; D046912:Multiprotein Complexes; D021382:Protein Sorting Signals; D015800:Protozoan Proteins; D016601:RNA-Binding Proteins