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Structural Basis for Phosphorylation-Dependent Recruitment of Tel2 to Hsp90 by Pih1

DOI: 10.1016/j.str.2014.04.001 DOI Help
PMID: 24794838 PMID Help

Authors: Mohinder Pal (MRC Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, U.K.) , Marc Morgan (MRC Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, U.K.) , Sarah e.l. Phelps (MRC Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, U.K.) , Mark Roe (MRC Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, U.K.) , Sarah Parry-morris (MRC Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, U.K.) , Jessica a. Downs (MRC Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, U.K.) , Sigrun Polier (MRC Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, U.K.) , Laurence h. Pearl (MRC Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, U.K.) , Chrisostomos Prodromou (MRC Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, U.K.)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Structure , VOL 22 (6) , PAGES 805 - 818

State: Published (Approved)
Published: June 2014
Diamond Proposal Number(s): 8015

Open Access Open Access

Abstract: Client protein recruitment to the Hsp90 system depends on cochaperones that bind the client and Hsp90 simultaneously and facilitate their interaction. Hsp90 involvement in the assembly of snoRNPs, RNA polymerases, PI3-kinase-like kinases, and chromatin remodeling complexes depends on the TTT (Tel2-Tti1-Tti2), and R2TP complexes—consisting of the AAA-ATPases Rvb1 and Rvb2, Tah1 (Spagh/RPAP3 in metazoa), and Pih1 (Pih1D1 in humans)—that together provide the connection to Hsp90. The biochemistry underlying R2TP function is still poorly understood. Pih1 in particular, at the heart of the complex, has not been described at a structural level, nor have the multiple protein-protein interactions it mediates been characterized. Here we present a structural and biochemical analysis of Hsp90-Tah1-Pih1, Hsp90-Spagh, and Pih1D1-Tel2 complexes that reveal a domain in Pih1D1 specific for binding CK2 phosphorylation sites, and together define the structural basis by which the R2TP complex connects the Hsp90 chaperone system to the TTT complex.

Subject Areas: Biology and Bio-materials


Instruments: I02-Macromolecular Crystallography , I03-Macromolecular Crystallography , I04-1-Macromolecular Crystallography (fixed wavelength) , I04-Macromolecular Crystallography

Added On: 29/09/2014 15:52

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