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 Jan 1 |
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ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology
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AU-rich element-mediated mRNA decay via the butyrate response factor 1 controls cellular levels of polyadenylated replication-dependent histone mRNAs. / Ryu, Incheol; Kim, Yoon Ki.
In: Journal of Biological Chemistry, Vol. 294, No. 19, 01.01.2019, p. 7558-7565.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - AU-rich element-mediated mRNA decay via the butyrate response factor 1 controls cellular levels of polyadenylated replication-dependent histone mRNAs
AU - Ryu, Incheol
AU - Kim, Yoon Ki
PY - 2019/1/1
Y1 - 2019/1/1
N2 - 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.
AB - 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.
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U2 - 10.1074/jbc.AC118.006766
DO - 10.1074/jbc.AC118.006766
M3 - Article
VL - 294
SP - 7558
EP - 7565
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 19
ER -