Comparative analysis of editosome proteins in trypanosomatids. Nucleic Acids Res 2003 Nov 15;31(22):6392-408
Date
11/07/2003Pubmed ID
14602897Pubmed Central ID
PMC275564DOI
10.1093/nar/gkg870Scopus ID
2-s2.0-0344668871 (requires institutional sign-in at Scopus site) 77 CitationsAbstract
Detailed comparisons of 16 editosome proteins from Trypanosoma brucei, Trypanosoma cruzi and Leishmania major identified protein motifs associated with catalysis and protein or nucleic acid interactions that suggest their functions in RNA editing. Five related proteins with RNase III-like motifs also contain a U1-like zinc finger and either dsRBM or Pumilio motifs. These proteins may provide the endoribonuclease function in editing. Two other related proteins, at least one of which is associated with U-specific 3' exonuclease activity, contain two putative nuclease motifs. Thus, editosomes contain a plethora of nucleases or proteins presumably derived from nucleases. Five additional related proteins, three of which have zinc fingers, each contain a motif associated with an OB fold; the TUTases have C-terminal folds reminiscent of RNA binding motifs, thus indicating the presence of numerous nucleic acid and/or protein binding domains, as do the two RNA ligases and a RNA helicase, which provide for additional catalytic steps in editing. These data indicate that trypanosomatid RNA editing is orchestrated by a variety of domains for catalysis, molecular interaction and structure. These domains are generally conserved within other protein families, but some are found in novel combinations in the editosome proteins.
Author List
Worthey EA, Schnaufer A, Mian IS, Stuart K, Salavati RMESH terms used to index this publication - Major topics in bold
AlgorithmsAmino Acid Motifs
Amino Acid Sequence
Animals
Leishmania major
Molecular Sequence Data
Protozoan Proteins
RNA Editing
RNA, Messenger
Ribonuclease III
Sequence Alignment
Sequence Homology, Amino Acid
Trypanosoma brucei brucei
Trypanosoma cruzi
Trypanosomatina
