Identification of novel components of Trypanosoma brucei editosomes

Aswini K Panigrahi, Achim Schnaufer, Nancy L Ernst, Bingbing Wang, Nicole Carmean, Reza Salavati, Kenneth Stuart

Research output: Contribution to journalArticlepeer-review

Abstract

The editosome is a multiprotein complex that catalyzes the insertion and deletion of uridylates that occurs during RNA editing in trypanosomatids. We report the identification of nine novel editosome proteins in Trypanosoma brucei. They were identified by mass spectrometric analysis of functional editosomes that were purified by serial ion exchange/gel permeation chromatography, immunoaffinity chromatography specific to the TbMP63 editosome protein, or tandem affinity purification based on a tagged RNA editing ligase. The newly identified proteins have ribonuclease and/or RNA binding motifs suggesting nuclease function for at least some of these. Five of the proteins are interrelated, as are two others, and one is related to four previously identified editosome proteins. The implications of these findings are discussed.
Original languageEnglish
Pages (from-to)484-92
Number of pages9
JournalRNA
Volume9
Issue number4
DOIs
Publication statusPublished - 2003

Keywords

  • RNA editing
  • protein
  • mass spectrometry
  • chromatography
  • TAP-tag
  • ribonuclease

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