Endoribonucleolytic Cleavage of m(6)A-Containing RNAs by RNase P/MRP Complex
- Authors
- Park, Ok Hyun; Ha, Hongseok; Lee, Yujin; Boo, Sung Ho; Kwon, Do Hoon; Song, Hyun Kyu; Kim, Yoon Ki
- Issue Date
- 2-May-2019
- Publisher
- CELL PRESS
- Keywords
- CCR4-NOT complex; circular RNA; endoribonucleolytic cleavage; FTO; HRSP12; m6A modification; METTL3; RNA decay; RNase P/MRP; YTHDF2
- Citation
- MOLECULAR CELL, v.74, no.3, pp.494 - +
- Indexed
- SCIE
SCOPUS
- Journal Title
- MOLECULAR CELL
- Volume
- 74
- Number
- 3
- Start Page
- 494
- End Page
- +
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/65465
- DOI
- 10.1016/j.molcel.2019.02.034
- ISSN
- 1097-2765
- 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.
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Collections - Graduate School > Department of Life Sciences > 1. Journal Articles
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