The Hsp90 chaperone controls the biogenesis of L7Ae RNPs through conserved machinery. - Archive ouverte HAL Access content directly
Journal Articles Journal of Cell Biology Year : 2008

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

Beáta E Jády
Benjamin Rothé
  • Function : Author
  • PersonId : 759789
  • IdRef : 161084079
Tamás Kiss
  • Function : Author
  • PersonId : 906442
Christine Allmang

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.
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Dates and versions

hal-00280860 , version 1 (28-05-2021)

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Séverine Boulon, Nathalie Marmier-Gourrier, Bérengère Pradet-Balade, Laurence Wurth, Céline Verheggen, et al.. The Hsp90 chaperone controls the biogenesis of L7Ae RNPs through conserved machinery.. Journal of Cell Biology, 2008, 180 (3), pp.579-95. ⟨10.1083/jcb.200708110⟩. ⟨hal-00280860⟩
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