Ontology highlight
ABSTRACT:
SUBMITTER: Zhao R
PROVIDER: S-EPMC2234237 | biostudies-literature | 2008 Feb
REPOSITORIES: biostudies-literature
Zhao Rongmin R Kakihara Yoshito Y Gribun Anna A Huen Jennifer J Yang Guocheng G Khanna May M Costanzo Michael M Brost Renée L RL Boone Charles C Hughes Timothy R TR Yip Christopher M CM Houry Walid A WA
The Journal of cell biology 20080201 3
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 ...[more]