A conserved PUF–Ago–eEF1A complex attenuates translation elongation
Copyright policy )A conserved PUF–Ago–eEF1A complex attenuates translation elongation
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.
- University of Wisconsin System United States
- UNIVERSITY OF WISCONSIN-MADISON United States
- University of Wisconsin–Madison United States
- University of Wisconsin–Oshkosh United States
- Howard Hughes Medical Institute United States
RNA-Binding Proteins, Article, Cell Line, Peptide Elongation Factor 1, Protein Biosynthesis, Argonaute Proteins, Animals, Humans, Eukaryotic Initiation Factors, Caenorhabditis elegans, Caenorhabditis elegans Proteins
RNA-Binding Proteins, Article, Cell Line, Peptide Elongation Factor 1, Protein Biosynthesis, Argonaute Proteins, Animals, Humans, Eukaryotic Initiation Factors, Caenorhabditis elegans, Caenorhabditis elegans Proteins
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