ArticleRNA (New York, N.Y.)2009
Differential functions of two editosome exoUases in 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 29 papers.
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Who cites it
29 citing papers in PubMed, 31 citations in OpenAlex.
- Pilot-Scale Screening of Clinically Approved Drugs to Identify Uridine Insertion/Deletion RNA Editing Inhibitors inACS infectious diseases · 2024Article
- 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
- KRGG1 function in RNA editing inRNA (New York, N.Y.) · 2023Article
- How RNases Shape Mitochondrial Transcriptomes.International journal of molecular sciences · 2022Review
- Lexis and Grammar of Mitochondrial RNA Processing in Trypanosomes.Trends in parasitology · 2020Review
- Editosome RNase III domain interactions are essential for editing and differ between life cycle stages inRNA (New York, N.Y.) · 2019Article
- 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
- Article
- Integrity of the core mitochondrial RNA-binding complex 1 is vital for trypanosome RNA editing.RNA (New York, N.Y.) · 2015Article
- Bloodstream form Trypanosoma brucei do not require mRPN1 for gRNA processing.RNA (New York, N.Y.) · 2015Article
- Review
- Trypanosoma brucei Tb927.2.6100 is an essential protein associated with kinetoplast DNA.Eukaryotic cell · 2013Article
- Inhibitors of RNA editing as potential chemotherapeutics against trypanosomatid pathogens.International journal for parasitology. Drugs and drug resistance · 2012Review
- Editosome accessory factors KREPB9 and KREPB10 in Trypanosoma brucei.Eukaryotic cell · 2012Article
- Crystal structure of a heterodimer of editosome interaction proteins in complex with two copies of a cross-reacting nanobody.Nucleic acids research · 2012Article
- Article
- Endonuclease associations with three distinct editosomes in Trypanosoma brucei.The Journal of biological chemistry · 2011Article
- Structures of a key interaction protein from the Trypanosoma brucei editosome in complex with single domain antibodies.Journal of structural biology · 2011Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Mitochondrial RNAs in trypanosomes are edited by the insertion and deletion of uridine (U) nucleotides to form translatable mRNAs. Editing is catalyzed by three distinct editosomes that contain two related U-specific exonucleases (exoUases), KREX1 and KREX2, with the former present exclusively in KREN1 editosomes and the latter present in all editosomes. We show here that repression of KREX1 expression leads to a concomitant reduction of KREN1 in approximately 20S editosomes, whereas KREX2 repression results in reductions of KREPA2 and KREL1 in approximately 20S editosomes. Knockdown of KREX1 results in reduced cell viability, reduction of some edited RNA in vivo, and a significant reduction in deletion but not insertion endonuclease activity in vitro. In contrast, KREX2 knockdown does not affect cell growth or editing in vivo but results in modest reductions of both insertion and deletion endonuclease activities and a significant reduction of U removal in vitro. Simultaneous knockdown of both proteins leads to a more severe inhibition of cell growth and editing in vivo and an additive effect on endonuclease cleavage in vitro. Taken together, these results indicate that both KREX1 and KREX2 are important for retention of other proteins in editosomes, and suggest that the reduction in cell viability upon KREX1 knockdown is likely a consequence of KREN1 loss. Furthermore, although KREX2 appears dispensable for cell growth, the increased inhibition of editing and parasite viability upon knockdown of both KREX1 and KREX2 together suggests that both proteins have roles in editing.
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Registered trials
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