期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 19, 期 2, 页码 176-183出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2214
关键词
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资金
- University of Wisconsin-Madison
- American Cancer Society [PF-10-127-01-DDC]
- US National Institutes of Health (NIH) [F32 GM095169]
- NIH [T32 GM07215, GM031892, GM050942, GM069454]
PUF (Pumilio/FBF) RNA-binding proteins and Argonaute (Ago) miRNA-binding proteins regulate mRNAs post-transcriptionally, each acting through similar, yet distinct, mechanisms. Here, we report that PUF and Ago proteins can also function together in a complex with a core translation elongation factor, eEF1A, to repress translation elongation. Both nematode (Caenorhabditis elegans) and mammalian PUF Ago eEF1A complexes were identified, using coimmunoprecipitation and recombinant protein assays. Nematode CSR-1 (Ago) promoted repression of FBF (PUF) target mRNAs in in vivo assays, and the FBF-1 CSR-1 heterodimer inhibited EFT-3 (eEF1A) GTPase activity in vitro. Mammalian PUM2-Ago-eEF1A inhibited translation of nonadenylated and polyadenylated reporter mRNAs in vitro. This repression occurred after translation initiation and led to ribosome accumulation within the open reading frame, roughly at the site where the nascent polypeptide emerged from the ribosomal exit tunnel. Together, these data suggest that a conserved PUF Ago eEF1A complex attenuates translation elongation.
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