Abstract
Replication-dependent histone (RDH) mRNAs have a nonpolyadenylated 3'-UTR that ends in a highly conserved stemloop structure. Nonetheless, a subset of RDH mRNAs has a poly(A) tail under physiological conditions. The biological meaning of poly(A)-containing (+) RDH mRNAs and details of their biosynthesis remain elusive. Here, using HeLa cells and Western blotting, qRT-PCR, and biotinylated RNA pulldown assays, we show that poly(A) + RDH mRNAs are post-transcriptionally regulated via adenylate- and uridylate-rich element-mediatedmRNAdecay (AMD).Weobserved that the rapid degradation of poly(A) + RDHmRNAis driven by butyrate response factor 1 (BRF1; also known as ZFP36 ring finger protein-like 1) under normal conditions. Conversely, cellular stresses such as UV C irradiation promoted BRF1 degradation, increased the association of Hu antigen R (HuR; also known as ELAV-like RNA-binding protein 1) with the 3'-UTR of poly(A)+ RDH mRNAs, and eventually stabilized the poly(A)+ RDH mRNAs. Collectively, our results provide evidence that AMD surveils poly(A)+ RDH mRNAs via BRF1-mediated degradation under physiological conditions.
Original language | English |
---|---|
Pages (from-to) | 7558-7565 |
Number of pages | 8 |
Journal | Journal of Biological Chemistry |
Volume | 294 |
Issue number | 19 |
DOIs | |
Publication status | Published - 2019 May 10 |
Bibliographical note
Publisher Copyright:© 2019 Ryu and Kim. Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc.
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology