REGULATION OF REPRESSIBLE ACID PHOSPHATASE BY CYCLIC AMP IN SACCHAROMYCES CEREVISIAE

Kunihiro Matsumoto ¹, Isao Uno ², and Tatsuo Ishikawa ²

¹ Department of Industrial Chemistry, Tottori University, Tottori-shi, Tottori 680, Japan
² Institute of Applied Microbiology, University of Tokyo, Bunkyo-ku, Tokyo 113, Japan

One of the cyr1 mutants (cyr1-2) in yeast produced low levels of adenylate cyclase and cyclic AMP at 25° and was unable to derepress acid phosphatase. Addition of cyclic AMP to the cyr1-2 cultures elevated the level of repressible acid phosphatase activity. The bcy1 mutation, which suppresses the cyr1-2 mutation by allowing activity of a cyclic AMP-independent protein kinase, also allows acid phosphatase synthesis without restoring adenylate cyclase activity. The CYR3 mutant had structurally altered cyclic AMP-dependent protein kinase and was unable to derepress acid phosphatase. The cyr1 locus was different from pho2, pho4 and pho81, which were known to regulate acid phosphatase synthesis. Mutants carrying cyr1-2 and pho80, PHO81^c, PHO82 or pho85 mutations, which confer constitutive synthesis of repressible acid phosphatase, produced acid phosphatase. The cyr1-2 mutant produced significantly low levels of invertase and - d-glucosidase. These results indicated that cyclic AMP-dependent protein kinase exerts its function in the synthesis of repressible acid phosphatase and other enzymes.

This article has been cited by other articles:

				H. Chautard, M. Jacquet, F. Schoentgen, N. Bureaud, and H. Benedetti Tfs1p, a Member of the PEBP Family, Inhibits the Ira2p but Not the Ira1p Ras GTPase-Activating Protein in Saccharomyces cerevisiae Eukaryot. Cell, April 1, 2004; 3(2): 459 - 470. [Abstract] [Full Text] [PDF]

				C. Liu, Z. Yang, J. Yang, Z. Xia, and S. Ao Regulation of the Yeast Transcriptional Factor PHO2 Activity by Phosphorylation J. Biol. Chem., October 6, 2000; 275(41): 31972 - 31978. [Abstract] [Full Text] [PDF]