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, e...

Descripción completa

Detalles Bibliográficos
Autores principales: Friend, Kyle, Campbell, Zachary T., Cooke, Amy, Kroll-Conner, Peggy, Wickens, Marvin P., Kimble, Judith
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2012
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3293257/
https://www.ncbi.nlm.nih.gov/pubmed/22231398
http://dx.doi.org/10.1038/nsmb.2214
_version_ 1782225384556724224
author Friend, Kyle
Campbell, Zachary T.
Cooke, Amy
Kroll-Conner, Peggy
Wickens, Marvin P.
Kimble, Judith
author_facet Friend, Kyle
Campbell, Zachary T.
Cooke, Amy
Kroll-Conner, Peggy
Wickens, Marvin P.
Kimble, Judith
author_sort Friend, Kyle
collection PubMed
description 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 and mammalian PUF/Ago/eEF1A complexes were identified, using co-immunoprecipitation and recombinant protein assays. Nematode CSR-1 (Ago) promotes repression of FBF (PUF) target mRNAs in in vivo assays, and the FBF-1/CSR-1 heterodimer inhibits EFT-3 (eEF1A) GTPase activity in vitro. Mammalian PUM2/Ago/eEF1A inhibits translation of nonadenylated and polyadenylated reporter mRNAs in vitro. This repression occurs after translation initiation and leads to ribosome accumulation within the open reading frame, roughly at the site where the nascent polypeptide emerges from the ribosomal exit tunnel. Together, these data suggest that a conserved PUF/Ago/eEF1A complex attenuates translation elongation.
format Online
Article
Text
id pubmed-3293257
institution National Center for Biotechnology Information
language English
publishDate 2012
record_format MEDLINE/PubMed
spelling pubmed-32932572012-08-01 A conserved PUF/Ago/eEF1A complex attenuates translation elongation Friend, Kyle Campbell, Zachary T. Cooke, Amy Kroll-Conner, Peggy Wickens, Marvin P. Kimble, Judith Nat Struct Mol Biol Article 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 and mammalian PUF/Ago/eEF1A complexes were identified, using co-immunoprecipitation and recombinant protein assays. Nematode CSR-1 (Ago) promotes repression of FBF (PUF) target mRNAs in in vivo assays, and the FBF-1/CSR-1 heterodimer inhibits EFT-3 (eEF1A) GTPase activity in vitro. Mammalian PUM2/Ago/eEF1A inhibits translation of nonadenylated and polyadenylated reporter mRNAs in vitro. This repression occurs after translation initiation and leads to ribosome accumulation within the open reading frame, roughly at the site where the nascent polypeptide emerges from the ribosomal exit tunnel. Together, these data suggest that a conserved PUF/Ago/eEF1A complex attenuates translation elongation. 2012-01-08 /pmc/articles/PMC3293257/ /pubmed/22231398 http://dx.doi.org/10.1038/nsmb.2214 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Friend, Kyle
Campbell, Zachary T.
Cooke, Amy
Kroll-Conner, Peggy
Wickens, Marvin P.
Kimble, Judith
A conserved PUF/Ago/eEF1A complex attenuates translation elongation
title A conserved PUF/Ago/eEF1A complex attenuates translation elongation
title_full A conserved PUF/Ago/eEF1A complex attenuates translation elongation
title_fullStr A conserved PUF/Ago/eEF1A complex attenuates translation elongation
title_full_unstemmed A conserved PUF/Ago/eEF1A complex attenuates translation elongation
title_short A conserved PUF/Ago/eEF1A complex attenuates translation elongation
title_sort conserved puf/ago/eef1a complex attenuates translation elongation
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3293257/
https://www.ncbi.nlm.nih.gov/pubmed/22231398
http://dx.doi.org/10.1038/nsmb.2214
work_keys_str_mv AT friendkyle aconservedpufagoeef1acomplexattenuatestranslationelongation
AT campbellzacharyt aconservedpufagoeef1acomplexattenuatestranslationelongation
AT cookeamy aconservedpufagoeef1acomplexattenuatestranslationelongation
AT krollconnerpeggy aconservedpufagoeef1acomplexattenuatestranslationelongation
AT wickensmarvinp aconservedpufagoeef1acomplexattenuatestranslationelongation
AT kimblejudith aconservedpufagoeef1acomplexattenuatestranslationelongation
AT friendkyle conservedpufagoeef1acomplexattenuatestranslationelongation
AT campbellzacharyt conservedpufagoeef1acomplexattenuatestranslationelongation
AT cookeamy conservedpufagoeef1acomplexattenuatestranslationelongation
AT krollconnerpeggy conservedpufagoeef1acomplexattenuatestranslationelongation
AT wickensmarvinp conservedpufagoeef1acomplexattenuatestranslationelongation
AT kimblejudith conservedpufagoeef1acomplexattenuatestranslationelongation

Ejemplares similares