Ca2+/calmodulin-activated protein phosphatase (PP2B) of Saccharomyces cerevisiae. PP2B activity is not essential for growth.
Protein phosphatase (PP2B) whose activity is stimulated 12-20-fold by Ca2+/calmodulin (CaM) was partially purified by CaM-Sepharose and heparin-agarose chromatographies from cell extract of the yeast Saccharomyces cerevisiae. PP2B activity was not detectable in a mutant in which two genes (CMP1 and CMP2) encoding homologs of mammalian PP2B catalytic subunit were disrupted. We have previously shown that the double gene disruption has no significant effect on the growth of yeast [1991, Mol. Gen. Genet. 227, 52-59]. The results indicated that CMP1 and CMP2 are the only genes that encode the PP2B catalytic polypeptide in S. cerevisiae, and PP2B activity is not essential for the growth of the yeast under normal conditions.
Nakamura
T
T
Department of Fermentation Technology, Faculty of Engineering, Hiroshima University, Japan.
Tsutsumi
H
H
Mukai
H
H
Kuno
T
T
Miyakawa
T
T
D002118:Calcium / Q000494:pharmacology; D002147:Calmodulin / Q000494:pharmacology; D002846:Chromatography, Affinity; D004533:Egtazic Acid / Q000494:pharmacology; D004988:Ethers, Cyclic / Q000494:pharmacology; D007700:Kinetics; D009154:Mutation; D019319:Okadaic Acid; D010749:Phosphoprotein Phosphatases / Q000302:isolation & purification / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000254:growth & development; D013045:Species Specificity
D002147:Calmodulin; D004988:Ethers, Cyclic; D019319:Okadaic Acid; D004533:Egtazic Acid; D010749:Phosphoprotein Phosphatases; D002118:Calcium