期刊
NUCLEIC ACIDS RESEARCH
卷 42, 期 11, 页码 6999-7011出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gku388
关键词
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资金
- Basic Science Research Program [2010-00252250, 2012R1A1A009809]
- Medical Research Center (MRC), National Research Foundation (NRF), Ministry of Education, Science and Technology (MEST), Republic of Korea [2008-0062190]
- Converging Research Center Program, Ministry of Science, ICT & Future Planning (MSIFP), Republic of Korea [2013K000283]
- Basic Science Research Program, NRF, MEST [2012R1A1A1009809]
- MRC, NRF, MEST [2008-0062190]
- Converging Research Center Program, MSIFP, Republic of Korea [2013K000283]
- National Research Foundation of Korea [2008-0062190, 2012R1A1A1009809] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
Requiem (REQ/DPF2) was originally identified as an apoptosis-inducing protein in mouse myeloid cells and belongs to the novel Kruppel-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, beta-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.
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