ArticlePhilosophical transactions of the Royal Society of London. Series B, Biological sciences2018
Human RNA cap1 methyltransferase CMTr1 cooperates with RNA helicase DHX15 to modify RNAs with highly structured 5' termini.
Article in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 27 citations in OpenAlex.
- RNA methyltransferase CMTR-1 inhibition activates a GATA transcription factor-mediated protective immune response.PLoS pathogens · 2026Article
- Cap-adjacent 2'-O-ribose methylation of RNA in C. elegans is required for postembryonic growth and germline development in the presence of the decapping exonuclease EOL-1.Nucleic acids research · 2026Article
- Loss of CMTR1 leads to gastrulation failure and early embryonic lethality.Developmental biology · 2025Article
- SNORA37/CMTR1/ELAVL1 feedback loop drives gastric cancer progression via facilitating CD44 alternative splicing.Journal of experimental & clinical cancer research : CR · 2025Article
- CK2 phosphorylation of CMTR1 promotes RNA cap formation and influenza virus infection.Cell reports · 2024Article
- CMTR-1 RNA methyltransferase mutations activate widespread expression of a dopaminergic neuron-specific mitochondrial complex I gene.Current biology : CB · 2024Article
- A helicase-independent role of DHX15 promotes MYC stability and acute leukemia cell survival.iScience · 2024Article
- The RNA cap methyltransferases RNMT and CMTR1 co-ordinate gene expression during neural differentiation.Biochemical Society transactions · 2023Review
- Regulation of the DEAH/RHA helicase Prp43 by the G-patch factor Pfa1.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The RNA helicase DHX15 is a critical regulator of natural killer-cell homeostasis and functions.Cellular & molecular immunology · 2022Article
- CMTR1 is recruited to transcription start sites and promotes ribosomal protein and histone gene expression in embryonic stem cells.Nucleic acids research · 2022Article
- CMTR1-Catalyzed 2'-O-Ribose Methylation Controls Neuronal Development by Regulating Camk2α Expression Independent of RIG-I Signaling.Cell reports · 2020Article
- The mRNA Cap 2'-mSphere · 2020Article
- 5' and 3' modifications controlling RNA degradation: from safeguards to executioners.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Article
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8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The 5'-cap structure, characteristic for RNA polymerase II-transcribed RNAs, plays important roles in RNA metabolism. In humans, RNA cap formation includes post-transcriptional modification of the first transcribed nucleotide by RNA cap1 methyltransferase (CMTr1). Here, we report that CMTr1 activity is hindered towards RNA substrates with highly structured 5' termini. We found that CMTr1 binds ATP-dependent RNA DHX15 helicase and that this interaction, mediated by the G-patch domain of CMTr1, has an advantageous effect on CMTr1 activity towards highly structured RNA substrates. The effect of DHX15 helicase activity is consistent with the strength of the secondary structure that has to be removed for CMTr1 to access the 5'-terminal residues in a single-stranded conformation. This is, to our knowledge, the first demonstration of the involvement of DHX15 in post-transcriptional RNA modification, and the first example of a molecular process in which DHX15 directly affects the activity of another enzyme. Our findings suggest a new mechanism underlying the regulatory role of DHX15 in the RNA capping process. RNAs with highly structured 5' termini constitute a significant fraction of the human transcriptome. Hence, CMTr1-DHX15 cooperation is likely to be important for the metabolism of RNA polymerase II-transcribed RNAs.This article is part of the theme issue '5' and 3' modifications controlling RNA degradation'.
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