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Worthey EA, Schnaufer A, Mian IS, et al. Comparative analysis of editosome proteins in trypanosomatids. Nucleic Acids Res. 2003;31(22):6392-408doi: 10.1093/nar/gkg870.
Worthey, E. A., Schnaufer, A., Mian, I. S., Stuart, K., & Salavati, R. (2003). Comparative analysis of editosome proteins in trypanosomatids. Nucleic acids research, 31(22), 6392-408. https://doi.org/10.1093/nar/gkg870
Worthey, Elizabeth A, et al. "Comparative analysis of editosome proteins in trypanosomatids." Nucleic acids research vol. 31,22 (2003): 6392-408. doi: https://doi.org/10.1093/nar/gkg870
Worthey EA, Schnaufer A, Mian IS, Stuart K, Salavati R. Comparative analysis of editosome proteins in trypanosomatids. Nucleic Acids Res. 2003 Nov 15;31(22):6392-408. doi: 10.1093/nar/gkg870. PMID: 14602897; PMCID: PMC275564.
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Nucleic Acids Res. 2003 Nov 15;31(22):6392-408. doi: 10.1093/nar/gkg870.

Comparative analysis of editosome proteins in trypanosomatids.

Nucleic acids research

Elizabeth A Worthey, Achim Schnaufer, I Saira Mian, Kenneth Stuart, Reza Salavati

Affiliations

  1. Seattle Biomedical Research Institute, Seattle, WA 98109, USA.

PMID: 14602897 PMCID: PMC275564 DOI: 10.1093/nar/gkg870

Abstract

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.

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