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Nucleic Acids Res. 2014 Jun;42(11):6999-7011. doi: 10.1093/nar/gku388. Epub 2014 May 5.

Staufen1-mediated mRNA decay induces Requiem mRNA decay through binding of Staufen1 to the Requiem 3'UTR.

Author information

  • 1Department of Life Science and Research Institute for Natural Sciences, College of Natural Sciences.
  • 2Graduate School for Biomedical Science and Engineering, Hanyang University, Seoul 133-791, Korea.
  • 3Department of Biotechnology, Konkuk University, Chungju 380-701, Korea.
  • 4Graduate School for Biomedical Science and Engineering, Hanyang University, Seoul 133-791, Korea jwhwang@hanyang.ac.kr.
  • 5Department of Life Science and Research Institute for Natural Sciences, College of Natural Sciences cgkim@hanyang.ac.kr.

Erratum in

  • Nucleic Acids Res. 2014;42(16):10871.

Abstract

Requiem (REQ/DPF2) was originally identified as an apoptosis-inducing protein in mouse myeloid cells and belongs to the novel Krüppel-type zinc finger d4-protein family of proteins, which includes neuro-d4 (DPF1) and cer-d4 (DPF3). Interestingly, when a portion of the REQ messenger ribonucleic acid (mRNA) 3' untranslated region (3'UTR), referred to as G8, was overexpressed in K562 cells, β-globin expression was induced, suggesting that the 3'UTR of REQ mRNA plays a physiological role. Here, we present evidence that the REQ mRNA 3'UTR, along with its trans-acting factor, Staufen1 (STAU1), is able to reduce the level of REQ mRNA via STAU1-mediated mRNA decay (SMD). By screening a complementary deoxyribonucleic acid (cDNA) expression library with an RNA-ligand binding assay, we identified STAU1 as an interactor of the REQ mRNA 3'UTR. Specifically, we provide evidence that STAU1 binds to putative 30-nucleotide stem-loop-structured RNA sequences within the G8 region, which we term the protein binding site core; this binding triggers the degradation of REQ mRNA and thus regulates translation. Furthermore, we demonstrate that siRNA-mediated silencing of either STAU1 or UPF1 increases the abundance of cellular REQ mRNA and, consequently, the REQ protein, indicating that REQ mRNA is a target of SMD.

© The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research.

PMID:
24799437
[PubMed - indexed for MEDLINE]
PMCID:
PMC4066795
Free PMC Article
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