Premium
Cdc37 maintains cellular viability in Schizosaccharomyces pombe independently of interactions with heat‐shock protein 90
Author(s) -
Turnbull Emma L.,
Martin Ina V.,
Fantes Peter A.
Publication year - 2005
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2005.04825.x
Subject(s) - cdc37 , schizosaccharomyces pombe , hsp90 , heat shock protein , chaperone (clinical) , saccharomyces cerevisiae , biology , hspa14 , microbiology and biotechnology , biochemistry , yeast , gene , hsp70 , medicine , pathology
Cdc37 is a molecular chaperone that interacts with a range of clients and co‐chaperones, forming various high molecular mass complexes. Cdc37 sequence homology among species is low. High homology between yeast and metazoan proteins is restricted to the extreme N‐terminal region, which is known to bind clients that are predominantly protein kinases. We show that despite the low homology, both Saccharomyces cerevisiae and human Cdc37 are able to substitute for the Schizosaccharomyces pombe protein in a strain deleted for the endogenous cdc37 gene. Expression of a construct consisting of only the N‐terminal domain of S. pombe Cdc37, lacking the postulated heat‐shock protein (Hsp) 90‐binding and homodimerization domains, can also sustain cellular viability, indicating that Cdc37 dimerization and interactions with the cochaperone Hsp90 may not be essential for Cdc37 function in S. pombe . Biochemical investigations showed that a small proportion of total cellular Cdc37 occurs in a high molecular mass complex that also contains Hsp90. These data indicate that the N‐terminal domain of Cdc37 carries out essential functions independently of the Hsp90‐binding domain and dimerization of the chaperone itself.