ArticleThe Journal of biological chemistry2010
A protein-protein interaction map of trypanosome ~20S editosomes.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 49 citations in OpenAlex.
- Article
- KREPA6 functions in RNA editing catalytic complex structural organization and gRNA utilization in Trypanosoma brucei.Nucleic acids research · 2026Article
- RNA editing catalytic complexes edit multiple mRNA sites non-processively in Trypanosoma brucei.Molecular and biochemical parasitology · 2023Article
- 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
- 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
- Lexis and Grammar of Mitochondrial RNA Processing in Trypanosomes.Trends in parasitology · 2020Review
- The OB-fold proteins of the Trypanosoma brucei editosome execute RNA-chaperone activity.Nucleic acids research · 2018Article
- The Architecture of Trypanosoma brucei editosomes.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- A Protein Complex Map of Trypanosoma brucei.PLoS neglected tropical diseases · 2016Article
- A novel high-throughput activity assay for the Trypanosoma brucei editosome enzyme REL1 and other RNA ligases.Nucleic acids research · 2016Article
- U-Insertion/Deletion mRNA-Editing Holoenzyme: Definition in Sight.Trends in parasitology · 2016Review
- Differential Editosome Protein Function between Life Cycle Stages of Trypanosoma brucei.The Journal of biological chemistry · 2015Article
- Structures of the T. brucei kRNA editing factor MRB1590 reveal unique RNA-binding pore motif contained within an ABC-ATPase fold.Nucleic acids research · 2015Article
- Mutational analysis of Trypanosoma brucei RNA editing ligase reveals regions critical for interaction with KREPA2.PloS one · 2015Article
- Review
- 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
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Mitochondrial mRNA editing in trypanosomatid parasites involves several multiprotein assemblies, including three very similar complexes that contain the key enzymatic editing activities and sediment at ~20S on glycerol gradients. These ~20S editosomes have a common set of 12 proteins, including enzymes for uridylyl (U) removal and addition, 2 RNA ligases, 2 proteins with RNase III-like domains, and 6 proteins with predicted oligonucleotide binding (OB) folds. In addition, each of the 3 distinct ~20S editosomes contains a different RNase III-type endonuclease, 1 of 3 related proteins and, in one case, an additional exonuclease. Here we present a protein-protein interaction map that was obtained through a combination of yeast two-hybrid analysis and subcomplex reconstitution with recombinant protein. This map interlinks ten of the proteins and in several cases localizes the protein region mediating the interaction, which often includes the predicted OB-fold domain. The results indicate that the OB-fold proteins form an extensive protein-protein interaction network that connects the two trimeric subcomplexes that catalyze U removal or addition and RNA ligation. One of these proteins, KREPA6, interacts with the OB-fold zinc finger protein in each subcomplex that interconnects their two catalytic proteins. Another OB-fold protein, KREPA3, appears to link to the putative endonuclease subcomplex. These results reveal a physical organization that underlies the coordination of the various catalytic and substrate binding activities within the ~20S editosomes during the editing process.
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