Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1.
Brighton, United Kingdom. In Structure, 2014
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 R2TP complex: discovery and functions.
Toronto, Canada. In Biochim Biophys Acta, 2012
It was found that Rvb1 and Rvb2 form a tight functional complex with Pih1 (Protein interacting with Hsp90) and Tah1 (TPR-containing protein associated with Hsp90), which are two Hsp90 interactors.
Hsp90: a chaperone for protein folding and gene regulation.
Toronto, Canada. In Biochem Cell Biol, 2005
We identified 2 highly conserved novel Hsp90 cofactors, termed Tah1 and Pih1, that bind to the chaperone and that also associate physically and functionally with the essential DNA helicases Rvb1 and Rvb2.