ArticleRNA (New York, N.Y.)2009
Novel TUTase associates with an editosome-like complex in mitochondria of Trypanosoma brucei.
Article in RNA (New York, N.Y.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 28 citations in OpenAlex.
- Article
- RNA editing catalytic complexes edit multiple mRNA sites non-processively in Trypanosoma brucei.Molecular and biochemical parasitology · 2023Article
- Dissecting Trypanosoma brucei RRP44 function in the maturation of segmented ribosomal RNA using a regulated genetic complementation system.Nucleic acids research · 2023Article
- Structural basis for guide RNA trimming by RNase D ribonuclease in Trypanosoma brucei.Nucleic acids research · 2021Article
- Lexis and Grammar of Mitochondrial RNA Processing in Trypanosomes.Trends in parasitology · 2020Review
- RNA Editing TUTase 1: structural foundation of substrate recognition, complex interactions and drug targeting.Nucleic acids research · 2016Article
- Constructive edge of uridylation-induced RNA degradation.RNA biology · 2016Review
- 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
- A critical switch in the enzymatic properties of the Cid1 protein deciphered from its product-bound crystal structure.Nucleic acids research · 2014Article
- Mutational analysis of Trypanosoma brucei editosome proteins KREPB4 and KREPB5 reveals domains critical for function.RNA (New York, N.Y.) · 2012Article
- Editosome accessory factors KREPB9 and KREPB10 in Trypanosoma brucei.Eukaryotic cell · 2012Article
- Article
- Mitochondrial RNA processing in trypanosomes.Research in microbiology · 2011Review
- Structure-function analysis of dynein light chain 1 identifies viable motility mutants in bloodstream-form Trypanosoma brucei.Eukaryotic cell · 2011Article
- Endonuclease associations with three distinct editosomes in Trypanosoma brucei.The Journal of biological chemistry · 2011Article
- A novel member of the RNase D exoribonuclease family functions in mitochondrial guide RNA metabolism in Trypanosoma brucei.The Journal of biological chemistry · 2011Article
- When you can't trust the DNA: RNA editing changes transcript sequences.Cellular and molecular life sciences : CMLS · 2011Review
- Mechanism of U insertion RNA editing in trypanosome mitochondria: the bimodal TUTase activity of the core complex.Journal of molecular biology · 2010Article
- Mechanism of U-insertion RNA editing in trypanosome mitochondria: characterization of RET2 functional domains by mutational analysis.Journal of molecular biology · 2010Article
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6 authors at 1 institution in 1 country.
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Abstract
Expression of mitochondrial genomes in Kinetoplastida protists requires massive uracil insertion/deletion mRNA editing. The cascade of editing reactions is accomplished by a multiprotein complex, the 20S editosome, and is directed by trans-acting guide RNAs. Two distinct RNA terminal uridylyl transferases (TUTases), RNA Editing TUTase 1 (RET1) and RNA Editing TUTase 2 (RET2), catalyze 3' uridylylation of guide RNAs and U-insertions into the mRNAs, respectively. RET1 is also involved in mitochondrial mRNA turnover and participates in numerous heterogeneous complexes; RET2 is an integral part of the 20S editosome, in which it forms a U-insertion subcomplex with zinc finger protein MP81 and RNA editing ligase REL2. Here we report the identification of a third mitochondrial TUTase from Trypanosoma brucei. The mitochondrial editosome-like complex associated TUTase (MEAT1) interacts with a 20S editosome-like particle, effectively substituting the U-insertion subcomplex. MEAT1 and RET2 are mutually exclusive in their respective complexes, which otherwise share several components. Similarly to RET2, MEAT1 is exclusively U-specific in vitro and is active on gapped double-stranded RNA resembling editing substrates. However, MEAT1 does not require a 5' phosphate group on the 3' mRNA cleavage fragment produced by editing endonucleases. The functional RNAi complementation experiments showed that MEAT1 is essential for viability of bloodstream and insect parasite forms. The growth inhibition phenotype in the latter can be rescued by coexpressing an RNAi-resistant gene with double-stranded RNA targeting the endogenous transcript. However, preliminary RNA analysis revealed no gross effects on RNA editing in MEAT1-depleted cells and indicated its possible role in regulating the mitochondrial RNA stability.
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