ArticleNucleic acids research2003
Comparative analysis of editosome proteins in trypanosomatids.
Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
What it found
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Who cites it
60 citing papers in PubMed, 88 citations in OpenAlex.
- KREPA6 functions in RNA editing catalytic complex structural organization and gRNA utilization in Trypanosoma brucei.Nucleic acids research · 2026Article
- Functional domain annotation by structural similarity.NAR genomics and bioinformatics · 2024Article
- Multiple domains of the integral KREPA3 protein are critical for the structure and precise functions of RNA editing catalytic complexes inRNA (New York, N.Y.) · 2023Article
- Circular mitochondrial-encoded mRNAs are a distinct subpopulation of mitochondrial mRNA in Trypanosoma brucei.Scientific reports · 2023Article
- Multiple domains of the integral KREPA3 protein are critical for the structure and precise functions of RNA Editing Catalytic Complexes inbioRxiv : the preprint server for biology · 2023Article
- The discovery and characterization of two novel structural motifs on the carboxy-terminal domain of kinetoplastid RNA editing ligases.RNA (New York, N.Y.) · 2023Article
- Conserved and transcript-specific functions of the RESC factors, RESC13 and RESC14, in kinetoplastid RNA editing.RNA (New York, N.Y.) · 2022Article
- Domain function and predicted structure of three heterodimeric endonuclease subunits of RNA editing catalytic complexes in Trypanosoma brucei.Nucleic acids research · 2022Article
- Sulfonated inhibitors of the RNA editing ligases validate the essential role of the MRP1/2 proteins in kinetoplastid RNA editing.RNA (New York, N.Y.) · 2020Article
- Editosome RNase III domain interactions are essential for editing and differ between life cycle stages inRNA (New York, N.Y.) · 2019Article
- The OB-fold proteins of the Trypanosoma brucei editosome execute RNA-chaperone activity.Nucleic acids research · 2018Article
- The essential functions of KREPB4 are developmentally distinct and required for endonuclease association with editosomes.RNA (New York, N.Y.) · 2017Article
- The Architecture of Trypanosoma brucei editosomes.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Investigating RNA editing factors from trypanosome mitochondria.Methods (San Diego, Calif.) · 2016Article
- Identification by Random Mutagenesis of Functional Domains in KREPB5 That Differentially Affect RNA Editing between Life Cycle Stages of Trypanosoma brucei.Molecular and cellular biology · 2015Article
- Differential Editosome Protein Function between Life Cycle Stages of Trypanosoma brucei.The Journal of biological chemistry · 2015Article
- Inhibitors of RNA editing as potential chemotherapeutics against trypanosomatid pathogens.International journal for parasitology. Drugs and drug resistance · 2012Review
- Explorations of linked editosome domains leading to the discovery of motifs defining conserved pockets in editosome OB-folds.Journal of structural biology · 2012Article
- Mutational analysis of Trypanosoma brucei editosome proteins KREPB4 and KREPB5 reveals domains critical for function.RNA (New York, N.Y.) · 2012Article
- The structure of the C-terminal domain of the largest editosome interaction protein and its role in promoting RNA binding by RNA-editing ligase L2.Nucleic acids research · 2012Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
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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