ArticleRNA (New York, N.Y.)2011
MRB3010 is a core component of the MRB1 complex that facilitates an early step of the kinetoplastid RNA editing process.
Article in RNA (New York, N.Y.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed.
- DRBD18 acts as a transcript-specific RNA editing auxiliary factor inRNA (New York, N.Y.) · 2025Article
- KRBP72 facilitates ATPase-dependent editing progression through a structural roadblock in mitochondrial A6 mRNA.Nucleic acids research · 2025Article
- KREH2 helicase represses ND7 mRNA editing in procyclic-stage Trypanosoma brucei by opposite modulation of canonical and 'moonlighting' gRNA utilization creating a proposed mRNA structure.Nucleic acids research · 2024Article
- RESC14 and RESC8 cooperate to mediate RESC function and dynamics during trypanosome RNA editing.Nucleic acids research · 2024Article
- KREH1 RNA helicase activity promotes utilization of initiator gRNAs across multiple mRNAs in trypanosome RNA editing.Nucleic acids research · 2023Article
- Structural basis for guide RNA selection by the RESC1-RESC2 complex.Nucleic acids research · 2023Article
- KRGG1 function in RNA editing inRNA (New York, N.Y.) · 2023Article
- Structure of the T. brucei kinetoplastid RNA editing substrate-binding complex core component, RESC5.PloS one · 2023Article
- Trypanosome RNAEditing Substrate Binding Complex integrity and function depends on the upstream action of RESC10.Nucleic acids research · 2021Article
- Nucleotide sugar biosynthesis occurs in the glycosomes of procyclic and bloodstream form Trypanosoma brucei.PLoS neglected tropical diseases · 2021Article
- Site-specific and substrate-specific control of accurate mRNA editing by a helicase complex in trypanosomes.RNA (New York, N.Y.) · 2020Article
- Developmental regulation of edited CYb and COIII mitochondrial mRNAs is achieved by distinct mechanisms in Trypanosoma brucei.Nucleic acids research · 2020Article
- 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
- Lexis and Grammar of Mitochondrial RNA Processing in Trypanosomes.Trends in parasitology · 2020Review
- MRB10130 is a RESC assembly factor that promotes kinetoplastid RNA editing initiation and progression.RNA (New York, N.Y.) · 2019Article
- Intrinsic and regulated properties of minimally edited trypanosome mRNAs.Nucleic acids research · 2019Article
- The RRM of the kRNA-editing protein TbRGG2 uses multiple surfaces to bind and remodel RNA.Nucleic acids research · 2019Article
- Protein features for assembly of the RNA editing helicase 2 subcomplex (REH2C) in Trypanosome holo-editosomes.PloS one · 2019Article
- Dynamic RNA holo-editosomes with subcomplex variants: Insights into the control of trypanosome editing.Wiley interdisciplinary reviews. RNA · 2018Review
- High throughput sequencing revolution reveals conserved fundamentals of U-indel editing.Wiley interdisciplinary reviews. RNA · 2018Review
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Abstract
Gene expression in the mitochondria of the kinetoplastid parasite Trypanosoma brucei is regulated primarily post-transcriptionally at the stages of RNA processing, editing, and turnover. The mitochondrial RNA-binding complex 1 (MRB1) is a recently identified multiprotein complex containing components with distinct functions during different aspects of RNA metabolism, such as guide RNA (gRNA) and mRNA turnover, precursor transcript processing, and RNA editing. In this study we examined the function of the MRB1 protein, Tb927.5.3010, which we term MRB3010. We show that MRB3010 is essential for growth of both procyclic form and bloodstream form life-cycle stages of T. brucei. Down-regulation of MRB3010 by RNAi leads to a dramatic inhibition of RNA editing, yet its depletion does not impact total gRNA levels. Rather, it appears to affect the editing process at an early stage, as indicated by the accumulation of pre-edited and small partially edited RNAs. MRB3010 is present in large (>20S) complexes and exhibits both RNA-dependent and RNA-independent interactions with other MRB1 complex proteins. Comparison of proteins isolated with MRB3010 tagged at its endogenous locus to those reported from other MRB1 complex purifications strongly suggests the presence of an MRB1 "core" complex containing five to six proteins, including MRB3010. Together, these data further our understanding of the function and composition of the imprecisely defined MRB1 complex.
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