Mass spectrometric analysis of the editosome and other multiprotein complexes in Trypanosoma brucei

Aswini K. Panigrahi, Thomas E. Allen, Kenneth Stuart*, Paul A. Haynes, Steven P. Gygi

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

52 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)728-735
Number of pages8
JournalJournal of the American Society for Mass Spectrometry
Volume14
Issue number7
DOIs
Publication statusPublished - Jul 2003
Externally publishedYes

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