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.
Bibliographical noteFunding Information:
This work was supported by National Research Foundation of Korea (NRF) Grant NRF-2015R1A3A2033665 funded by the Korea government (Ministry of Science, ICT and Future Planning) and by a Korea University grant
This work was supported by National Research Foundation of Korea (NRF) Grant NRF-2015R1A3A2033665 funded by the Korea government (Minis-try of Science, ICT and Future Planning) and by a Korea University grant. The authors declare that they have no conflicts of interest with the con-tents of this article.
© 2019 Ryu and Kim. Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc.
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology