Identification of novel components of Trypanosoma brucei editosomes.
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.
Panigrahi
Aswini K
AK
Seattle Biomedical Research Institute, Seattle, Washington 98109, USA.
Schnaufer
Achim
A
Ernst
Nancy L
NL
Wang
Bingbing
B
Carmean
Nicole
N
Salavati
Reza
R
Stuart
Kenneth
K
D000595:Amino Acid Sequence; D000818:Animals; D002853:Chromatography, Liquid; D046911:Macromolecular Substances; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D046912:Multiprotein Complexes; D017393:RNA Editing / Q000502:physiology*; D016601:RNA-Binding Proteins / Q000737:chemistry*; D017422:Sequence Analysis, DNA; D014346:Trypanosoma brucei brucei / Q000737:chemistry* / Q000235:genetics* / Q000502:physiology
D046911:Macromolecular Substances; D046912:Multiprotein Complexes; D016601:RNA-Binding Proteins