Endoribonucleolytic cleavage of m6A-containing RNAs by RNase P/MRP complex. Park et al
| Main Author: | Kim, Yoon Ki |
|---|---|
| Format: | Dataset |
| Terbitan: |
Mendeley
, 2019
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| Subjects: | |
| Online Access: |
https:/data.mendeley.com/datasets/rxjghsgczt |
Daftar Isi:
- N6-methyladenosine (m6A) 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 m6A-mediated gene regulation is poorly understood. Here, we show that m6A-containing RNAs are subject to endoribonucleolytic cleavage via YTHDF2 (m6A 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 m6A RNAs that are preferentially targeted for endoribonucleolytic cleavage have an HRSP12-binding site and RNase P/MRP-directed cleavage site, respectively, upstream and downstream of the YTHDF2-binding site. We also find that a subset of m6A-containing circular RNAs associate with YTHDF2 in an HRSP12-dependent manner and are selectively downregulated by RNase P/MRP. Thus, our data expand the known functions of RNase P/MRP to endoribonucleolytic cleavage of m6A RNAs.