Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation.

Hsp90 is a highly conserved molecular chaperone that is involved in modulating a multitude of cellular processes. In this study, we identify a function for the chaperone in RNA processing and maintenance. This functionality of Hsp90 involves two recently identified interactors of the chaperone: Tah1 and Pih1/Nop17. Tah1 is a ...
small protein containing tetratricopeptide repeats, whereas Pih1 is found to be an unstable protein. Tah1 and Pih1 bind to the essential helicases Rvb1 and Rvb2 to form the R2TP complex, which we demonstrate is required for the correct accumulation of box C/D small nucleolar ribonucleoproteins. Together with the Tah1 cofactor, Hsp90 functions to stabilize Pih1. As a consequence, the chaperone is shown to affect box C/D accumulation and maintenance, especially under stress conditions. Hsp90 and R2TP proteins are also involved in the proper accumulation of box H/ACA small nucleolar RNAs.
Mesh Terms:
Adenosine Triphosphatases, Cell Cycle Proteins, DNA Helicases, DNA-Binding Proteins, Gene Expression Regulation, Fungal, HSP90 Heat-Shock Proteins, Macromolecular Substances, Molecular Chaperones, Nuclear Proteins, Protein Folding, RNA Processing, Post-Transcriptional, RNA, Small Nucleolar, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Transcription Factors
J. Cell Biol.
Date: Feb. 11, 2008
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