{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Toczydlowska-Socha D"],"funding":["Fundacja na rzecz Nauki Polskiej","European Research Council","Narodowe Centrum Nauki"],"pagination":["20180161"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6232587"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["373(1762)"],"pubmed_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"],"journal":["Philosophical transactions of the Royal Society of London. Series B, Biological sciences"],"pubmed_title":["Human RNA cap1 methyltransferase CMTr1 cooperates with RNA helicase DHX15 to modify RNAs with highly structured 5' termini."],"pmcid":["PMC6232587"],"funding_grant_id":["261351","TEAM/2009–4/2","2011/03/D/NZ1/03247","MISTRZ/1./2014","2017/24/T/NZ1/00170","2015/19/N/NZ1/03449"],"pubmed_authors":["Toczydlowska-Socha D","Stefaniak F","Zielinska MM","Astha","Almeida CF","Bujnicki JM","Kurkowska M","Purta E"],"additional_accession":[]},"is_claimable":false,"name":"Human RNA cap1 methyltransferase CMTr1 cooperates with RNA helicase DHX15 to modify RNAs with highly structured 5' termini.","description":"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","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Nov","modification":"2025-04-19T15:00:40.9Z","creation":"2019-03-26T22:40:55Z"},"accession":"S-EPMC6232587","cross_references":{"pubmed":["30397098"],"doi":["10.1098/rstb.2018.0161"]}}