PIH1 cDNA ORF clone, Saccharomyces cerevisiae S288C

Life with 6000 genes.
Goffeau A, Barrell BG, Bussey H, Davis RW, Dujon B, Feldmann H, Galibert F, Hoheisel JD, Jacq C, Johnston M, Louis EJ, Mewes HW, Murakami Y, Philippsen P, Tettelin H, Oliver SG
Science (New York, N.Y.)274(5287)546, 563-7(1996 Oct)

Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII.
Johnston M, Andrews S, Brinkman R, Cooper J, Ding H, Dover J, Du Z, Favello A, Fulton L, Gattung S
Science (New York, N.Y.)265(5181)2077-82(1994 Sep)

Results show that Nop17 interacts with the C-terminal portion of Nop58, affecting its affinity for snoRNA, Nop58 stability, and the localization of the box C/D snoRNP components, indicating a key role played by Nop17 in snoRNP assembly.
Title: Nop17 is a key R2TP factor for the assembly and maturation of box C/D snoRNP complex.

Results show that Nop58 strongly interacts with the R2TP complex through its interaction with Pih1 resulting in Nop58 stabilization.
Title: Nutritional status modulates box C/D snoRNP biogenesis by regulated subcellular relocalization of the R2TP complex.

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
Title: Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1.

The Tah1 C-terminal region is unfolded, and is essential for the recruitment of the Pih1 C-terminal domain and folds upon binding.
Title: High-resolution structural analysis shows how Tah1 tethers Hsp90 to the R2TP complex.

The stability of the small nucleolar ribonucleoprotein (snoRNP) assembly protein Pih1 in Saccharomyces cerevisiae is modulated by its C terminus.
Title: The stability of the small nucleolar ribonucleoprotein (snoRNP) assembly protein Pih1 in Saccharomyces cerevisiae is modulated by its C terminus.