ArticleRNA (New York, N.Y.)2012
Mutational analysis of Trypanosoma brucei editosome proteins KREPB4 and KREPB5 reveals domains critical for function.
Article in RNA (New York, N.Y.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 25 citations in OpenAlex.
- Deep mutational scanning of the RNase III-like domain inFrontiers in cellular and infection microbiology · 2024Article
- RNA editing catalytic complexes edit multiple mRNA sites non-processively in Trypanosoma brucei.Molecular and biochemical parasitology · 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
- How RNases Shape Mitochondrial Transcriptomes.International journal of molecular sciences · 2022Review
- Lexis and Grammar of Mitochondrial RNA Processing in Trypanosomes.Trends in parasitology · 2020Review
- Article
- Editosome RNase III domain interactions are essential for editing and differ between life cycle stages inRNA (New York, N.Y.) · 2019Article
- MRB7260 is essential for productive protein-RNA interactions within the RNA editing substrate binding complex during trypanosome RNA editing.RNA (New York, N.Y.) · 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
- U-Insertion/Deletion mRNA-Editing Holoenzyme: Definition in Sight.Trends in parasitology · 2016Review
- 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
- Bloodstream form Trypanosoma brucei do not require mRPN1 for gRNA processing.RNA (New York, N.Y.) · 2015Article
- Review
- Genetic validation of aminoacyl-tRNA synthetases as drug targets in Trypanosoma brucei.Eukaryotic cell · 2014Article
- A multiple aminoacyl-tRNA synthetase complex that enhances tRNA-aminoacylation in African trypanosomes.Molecular and cellular biology · 2013Article
- A spectrophotometric assay for quantitative measurement of aminoacyl-tRNA synthetase activity.Journal of biomolecular screening · 2013Article
- Stunning Intricacies of RNA Editing Complexes RECC, RESC, and REH2C: Functional Organization, Developmental Regulation, and Evolutionary History in Kinetoplastid Protists.Wiley interdisciplinary reviews. RNAReview
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
The transcriptome of kinetoplastid mitochondria undergoes extensive RNA editing that inserts and deletes uridine residues (U's) to produce mature mRNAs. The editosome is a multiprotein complex that provides endonuclease, TUTase, exonuclease, and ligase activities required for RNA editing. The editosome's KREPB4 and KREPB5 proteins are essential for editosome integrity and parasite viability and contain semi-conserved motifs corresponding to zinc finger, RNase III, and PUF domains, but to date no functional analysis of these domains has been reported. We show here that various point mutations to KREPB4 and KREPB5 identify essential domains, and suggest that these proteins do not themselves perform RNase III catalysis. The zinc finger of KREPB4 but not KREPB5 is essential for editosome integrity and parasite viability, and mutation of the RNase III signature motif in KREPB5 prevents integration into editosomes, which is lethal. Isolated TAP-tagged KREPB4 and KREPB5 complexes preferentially associate with components of the deletion subcomplex, providing additional insights into editosome architecture. A new alignment of editosome RNase III sequences from several kinetoplastid species implies that KREPB4 and KREPB5 lack catalytic activity and reveals that the PUF motif is present in the editing endonucleases KREN1, KREN2, and KREN3. The data presented here are consistent with the hypothesis that KREPB4 and KREPB5 form intermolecular heterodimers with the catalytically active editing endonucleases, which is unprecedented among known RNase III proteins.
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