DC Field | Value | Language |
---|---|---|
dc.contributor.author | Park, Ok Hyun | ko |
dc.contributor.author | Ha, Hongseok | ko |
dc.contributor.author | Lee, Yujin | ko |
dc.contributor.author | Boo, Sung Ho | ko |
dc.contributor.author | Kwon, Do Hoon | ko |
dc.contributor.author | Song, Hyun Kyu | ko |
dc.contributor.author | Kim, Yoon Ki | ko |
dc.date.accessioned | 2022-08-04T05:00:33Z | - |
dc.date.available | 2022-08-04T05:00:33Z | - |
dc.date.created | 2022-08-04 | - |
dc.date.created | 2022-08-04 | - |
dc.date.created | 2022-08-04 | - |
dc.date.created | 2022-08-04 | - |
dc.date.issued | 2019-05 | - |
dc.identifier.citation | MOLECULAR CELL, v.74, no.3, pp.494 - 507 | - |
dc.identifier.issn | 1097-2765 | - |
dc.identifier.uri | http://hdl.handle.net/10203/297741 | - |
dc.description.abstract | N-6-methyladenosine (m(6)A) is the most abundant internal modification in RNAs and plays regulatory roles in a variety of biological and physiological processes. Despite its important roles, the molecular mechanism underlying m(6)A-mediated gene regulation is poorly understood. Here, we show that m(6)A-containing RNAs are subject to endoribonucleolytic cleavage via YTHDF2 (m(6)A reader protein), HRSP12 (adaptor protein), and RNase P/MRP (endoribonucleases). We demonstrate that HRSP12 functions as an adaptor to bridge YTHDF2 and RNase P/MRP, eliciting rapid degradation of YTHDF2-bound RNAs. Transcriptome-wide analyses show that m(6)A RNAs that are preferentially targeted for endoribonucleolytic cleavage have an HRSP12-binding site and a RNase P/MRP-directed cleavage site upstream and downstream of the YTHDF2-binding site, respectively. We also find that a subset of m(6)A-containing circular RNAs associates with YTHDF2 in an HRSP12-dependent manner and is selectively downregulated by RNase P/MRP. Thus, our data expand the known functions of RNase P/MRP to endoribonucleolytic cleavage of m(6)A RNAs. | - |
dc.language | English | - |
dc.publisher | CELL PRESS | - |
dc.title | Endoribonucleolytic Cleavage of m(6)A-Containing RNAs by RNase P/MRP Complex | - |
dc.type | Article | - |
dc.identifier.wosid | 000466703900010 | - |
dc.identifier.scopusid | 2-s2.0-85064865187 | - |
dc.type.rims | ART | - |
dc.citation.volume | 74 | - |
dc.citation.issue | 3 | - |
dc.citation.beginningpage | 494 | - |
dc.citation.endingpage | 507 | - |
dc.citation.publicationname | MOLECULAR CELL | - |
dc.identifier.doi | 10.1016/j.molcel.2019.02.034 | - |
dc.contributor.localauthor | Kim, Yoon Ki | - |
dc.contributor.nonIdAuthor | Park, Ok Hyun | - |
dc.contributor.nonIdAuthor | Ha, Hongseok | - |
dc.contributor.nonIdAuthor | Lee, Yujin | - |
dc.contributor.nonIdAuthor | Boo, Sung Ho | - |
dc.contributor.nonIdAuthor | Kwon, Do Hoon | - |
dc.contributor.nonIdAuthor | Song, Hyun Kyu | - |
dc.description.isOpenAccess | N | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | IDENTIFICATION | - |
dc.subject.keywordPlus | TRANSLATION | - |
dc.subject.keywordPlus | REVEALS | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | ROLES | - |
dc.subject.keywordPlus | SITES | - |
dc.subject.keywordPlus | NMD | - |
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