ArticleMolecular and biochemical parasitology2007
Targeted depletion of a mitochondrial nucleotidyltransferase suggests the presence of multiple enzymes that polymerize mRNA 3' tails in Trypanosoma brucei mitochondria.
Article in Molecular and biochemical parasitology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 22 citations in OpenAlex.
- Circular mitochondrial-encoded mRNAs are a distinct subpopulation of mitochondrial mRNA in Trypanosoma brucei.Scientific reports · 2023Article
- Circular mitochondrial-encoded mRNAs are a distinct subpopulation of mitochondrial mRNA inbioRxiv : the preprint server for biology · 2023Article
- Manipulation of mitochondrial poly(A) polymerase family proteins inFrontiers in parasitology · 2023Article
- Probabilistic models of biological enzymatic polymerization.PloS one · 2021Article
- Lexis and Grammar of Mitochondrial RNA Processing in Trypanosomes.Trends in parasitology · 2020Review
- Constructive edge of uridylation-induced RNA degradation.RNA biology · 2016Review
- circTAIL-seq, a targeted method for deep analysis of RNA 3' tails, reveals transcript-specific differences by multiple metrics.RNA (New York, N.Y.) · 2016Article
- An arginine-glycine-rich RNA binding protein impacts the abundance of specific mRNAs in the mitochondria of Trypanosoma brucei.Eukaryotic cell · 2015Article
- Article
- Mitochondrial RNA processing in trypanosomes.Research in microbiology · 2011Review
- A novel member of the RNase D exoribonuclease family functions in mitochondrial guide RNA metabolism in Trypanosoma brucei.The Journal of biological chemistry · 2011Article
- Structure of the mitochondrial editosome-like complex associated TUTase 1 reveals divergent mechanisms of UTP selection and domain organization.Journal of molecular biology · 2010Article
- Distinct and overlapping functions of MRP1/2 and RBP16 in mitochondrial RNA metabolism.Molecular and cellular biology · 2009Article
- Novel TUTase associates with an editosome-like complex in mitochondria of Trypanosoma brucei.RNA (New York, N.Y.) · 2009Article
- Identification and characterization of nuclear non-canonical poly(A) polymerases from Trypanosoma brucei.Molecular and biochemical parasitology · 2009Article
- New perspectives on the diversification of the RNA interference system: insights from comparative genomics and small RNA sequencing.Wiley interdisciplinary reviews. RNAReview
- Mitochondrial poly(A) polymerase and polyadenylation.Biochimica et biophysica actaReview
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2 authors at 1 institution in 1 country.
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Abstract
Polyadenylation plays an important role in regulating RNA stability in Trypanosoma brucei mitochondria. To date, little is known about the enzymes responsible for the addition of mRNA 3' tails in this system. In this study, we characterize a trypanosome homolog of the human mitochondrial poly(A) polymerase, which we term kPAP2. kPAP2 is mitochondrially localized and expressed in both bloodstream and procyclic form trypanosomes. Targeted gene depletion using RNAi showed that kPAP2 is not required for T. brucei growth in either bloodstream or procyclic life stages, nor is it essential for differentiation from bloodstream to procyclic form. We also demonstrate that steady state abundance of several mitochondrial RNAs was largely unaffected upon kPAP2 down-regulation. Interestingly, mRNA 3' tail analysis of several mRNAs from both life cycle stages in uninduced kPAP2 RNAi cells demonstrated that tail length and uridine content are both regulated in a transcript-specific manner. mRNA-specific tail lengths were maintained upon kPAP2 depletion. However, the percentage of uridine residues in 3' tails was increased, and conversely the percentage of adenosine residues was decreased, in a distinct subset of mRNAs when kPAP2 levels were down-regulated. Thus, kPAP2 apparently contributes to the incorporation of adenosine residues in 3' tails of some, but not all, mitochondrial mRNAs. Together, these data suggest that multiple nucleotidyltransferases act on mitochondrial mRNA 3' ends, and that these enzymes are somewhat redundant and subject to complex regulation.
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