The Hsp90 chaperone controls the biogenesis of L7Ae RNPs through conserved machinery

Author:

Boulon Séverine1,Marmier-Gourrier Nathalie2,Pradet-Balade Bérengère1,Wurth Laurence3,Verheggen Céline1,Jády Beáta E.4,Rothé Benjamin2,Pescia Christina1,Robert Marie-Cécile1,Kiss Tamás4,Bardoni Barbara5,Krol Alain3,Branlant Christiane2,Allmang Christine3,Bertrand Edouard1,Charpentier Bruno2

Affiliation:

1. Institute of Molecular Genetics of Montpellier, Centre National de la Recherche Scientifique, Unité Mixte de Recherche 5535, Montpellier Cedex 5, France

2. Maturation des ARN et Enzymologie Moléculaire, Unité Mixte de Recherche 7567, Centre National de la Recherche Scientifique, Université Henri Poincaré, Nancy Université, Faculté des Sciences et Techniques, 54506 Vandoeuvre-les-Nancy, France

3. Architecture et Réactivité de l'ARN, Université Louis Pasteur de Strasbourg, Centre National de la Recherche Scientifique, Institut de Biologie Moléculaire et Cellulaire, 67084 Strasbourg, France

4. Laboratoire de Biologie Moléculaire Eucaryote, Université Paul Sabatier, 31062 Toulouse, France

5. Institute of Genetics and Molecular and Cellular Biology, 67404 Illkirch, France

Abstract

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.

Publisher

Rockefeller University Press

Subject

Cell Biology

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