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The Hsp90 chaperone controls the biogenesis of L7Ae RNPs through conserved machinery
RNA-binding proteins of the L7Ae family are at the heart of many essential ribonucleoproteins (RNPs), including box C/D and H/ACA small nucleolar RNPs, U4 small nuclear RNP, telomerase, and messenger RNPs coding for selenoproteins. In this study, we show that Nufip and its yeast homologue Rsa1 are k...
Autores principales: | , , , , , , , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2008
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2234240/ https://www.ncbi.nlm.nih.gov/pubmed/18268104 http://dx.doi.org/10.1083/jcb.200708110 |
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author | Boulon, Séverine Marmier-Gourrier, Nathalie Pradet-Balade, Bérengère Wurth, Laurence Verheggen, Céline Jády, Beáta E. Rothé, Benjamin Pescia, Christina Robert, Marie-Cécile Kiss, Tamás Bardoni, Barbara Krol, Alain Branlant, Christiane Allmang, Christine Bertrand, Edouard Charpentier, Bruno |
author_facet | Boulon, Séverine Marmier-Gourrier, Nathalie Pradet-Balade, Bérengère Wurth, Laurence Verheggen, Céline Jády, Beáta E. Rothé, Benjamin Pescia, Christina Robert, Marie-Cécile Kiss, Tamás Bardoni, Barbara Krol, Alain Branlant, Christiane Allmang, Christine Bertrand, Edouard Charpentier, Bruno |
author_sort | Boulon, Séverine |
collection | PubMed |
description | RNA-binding proteins of the L7Ae family are at the heart of many essential ribonucleoproteins (RNPs), including box C/D and H/ACA small nucleolar RNPs, U4 small nuclear RNP, telomerase, and messenger RNPs coding for selenoproteins. In this study, we show that Nufip and its yeast homologue Rsa1 are key components of the machinery that assembles these RNPs. We observed that Rsa1 and Nufip bind several L7Ae proteins and tether them to other core proteins in the immature particles. Surprisingly, Rsa1 and Nufip also link assembling RNPs with the AAA + adenosine triphosphatases hRvb1 and hRvb2 and with the Hsp90 chaperone through two conserved adaptors, Tah1/hSpagh and Pih1. Inhibition of Hsp90 in human cells prevents the accumulation of U3, U4, and telomerase RNAs and decreases the levels of newly synthesized hNop58, hNHP2, 15.5K, and SBP2. Thus, Hsp90 may control the folding of these proteins during the formation of new RNPs. This suggests that Hsp90 functions as a master regulator of cell proliferation by allowing simultaneous control of cell signaling and cell growth. |
format | Text |
id | pubmed-2234240 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-22342402008-08-11 The Hsp90 chaperone controls the biogenesis of L7Ae RNPs through conserved machinery Boulon, Séverine Marmier-Gourrier, Nathalie Pradet-Balade, Bérengère Wurth, Laurence Verheggen, Céline Jády, Beáta E. Rothé, Benjamin Pescia, Christina Robert, Marie-Cécile Kiss, Tamás Bardoni, Barbara Krol, Alain Branlant, Christiane Allmang, Christine Bertrand, Edouard Charpentier, Bruno J Cell Biol Research Articles RNA-binding proteins of the L7Ae family are at the heart of many essential ribonucleoproteins (RNPs), including box C/D and H/ACA small nucleolar RNPs, U4 small nuclear RNP, telomerase, and messenger RNPs coding for selenoproteins. In this study, we show that Nufip and its yeast homologue Rsa1 are key components of the machinery that assembles these RNPs. We observed that Rsa1 and Nufip bind several L7Ae proteins and tether them to other core proteins in the immature particles. Surprisingly, Rsa1 and Nufip also link assembling RNPs with the AAA + adenosine triphosphatases hRvb1 and hRvb2 and with the Hsp90 chaperone through two conserved adaptors, Tah1/hSpagh and Pih1. Inhibition of Hsp90 in human cells prevents the accumulation of U3, U4, and telomerase RNAs and decreases the levels of newly synthesized hNop58, hNHP2, 15.5K, and SBP2. Thus, Hsp90 may control the folding of these proteins during the formation of new RNPs. This suggests that Hsp90 functions as a master regulator of cell proliferation by allowing simultaneous control of cell signaling and cell growth. The Rockefeller University Press 2008-02-11 /pmc/articles/PMC2234240/ /pubmed/18268104 http://dx.doi.org/10.1083/jcb.200708110 Text en Copyright © 2008, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Research Articles Boulon, Séverine Marmier-Gourrier, Nathalie Pradet-Balade, Bérengère Wurth, Laurence Verheggen, Céline Jády, Beáta E. Rothé, Benjamin Pescia, Christina Robert, Marie-Cécile Kiss, Tamás Bardoni, Barbara Krol, Alain Branlant, Christiane Allmang, Christine Bertrand, Edouard Charpentier, Bruno The Hsp90 chaperone controls the biogenesis of L7Ae RNPs through conserved machinery |
title | The Hsp90 chaperone controls the biogenesis of L7Ae RNPs through conserved machinery |
title_full | The Hsp90 chaperone controls the biogenesis of L7Ae RNPs through conserved machinery |
title_fullStr | The Hsp90 chaperone controls the biogenesis of L7Ae RNPs through conserved machinery |
title_full_unstemmed | The Hsp90 chaperone controls the biogenesis of L7Ae RNPs through conserved machinery |
title_short | The Hsp90 chaperone controls the biogenesis of L7Ae RNPs through conserved machinery |
title_sort | hsp90 chaperone controls the biogenesis of l7ae rnps through conserved machinery |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2234240/ https://www.ncbi.nlm.nih.gov/pubmed/18268104 http://dx.doi.org/10.1083/jcb.200708110 |
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