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Genetics, Vol. 178, 1927-1936, April 2008, Copyright © 2008
doi:10.1534/genetics.107.086165

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Schizosaccharomyces pombe Hsp90/Git10 Is Required for Glucose/cAMP Signaling

Manal A. Alaamery and Charles S. Hoffman1

Biology Department, Boston College, Chestnut Hill, Massachusetts 02467

1 Corresponding author: Biology Department, Boston College, Higgins Hall 401B, 140 Commonwealth Ave., Chestnut Hill, MA 02467.
E-mail: hoffmacs{at}bc.edu

The fission yeast Schizosaccharomyces pombe senses environmental glucose through a cAMP-signaling pathway. Elevated cAMP levels activate protein kinase A (PKA) to inhibit transcription of genes involved in sexual development and gluconeogenesis, including the fbp1+ gene, which encodes fructose-1,6-bisphosphatase. Glucose-mediated activation of PKA requires the function of nine glucose-insensitive transcription (git) genes, encoding adenylate cyclase, the PKA catalytic subunit, and seven "upstream" proteins required for glucose-triggered adenylate cyclase activation. We describe the cloning and characterization of the git10+ gene, which is identical to swo1+ and encodes the S. pombe Hsp90 chaperone protein. Glucose repression of fbp1+ transcription is impaired by both git10– and swo1– mutant alleles of the hsp90+ gene, as well as by chemical inhibition of Hsp90 activity and temperature stress to wild-type cells. Unlike the swo1– mutant alleles, the git10-201 allele supports cell growth at 37°, while severely reducing glucose repression of an fbp1-lacZ reporter, suggesting a separation-of-function defect. Sequence analyses of three swo1– alleles and the one git10– allele indicate that swo1– mutations alter core functional domains of Hsp90, while the git10– mutation affects the Hsp90 central domain involved in client protein binding. These results suggest that Hsp90 plays a specific role in the S. pombe glucose/cAMP pathway.






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