Nakamura T, Tsutsumi H, Mukai H, Kuno T, Miyakawa T
Department of Fermentation Technology, Faculty of Engineering, Hiroshima University, Japan.
FEBS Lett. 1992 Aug 31;309(1):103-6. doi: 10.1016/0014-5793(92)80749-7.
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.
蛋白磷酸酶(PP2B)的活性受Ca2+/钙调蛋白(CaM)刺激12至20倍,通过CaM-琼脂糖凝胶和肝素-琼脂糖凝胶色谱法从酿酒酵母的细胞提取物中进行了部分纯化。在一个破坏了编码哺乳动物PP2B催化亚基同源物的两个基因(CMP1和CMP2)的突变体中未检测到PP2B活性。我们之前已经表明,双基因破坏对酵母的生长没有显著影响[1991年,《分子与普通遗传学》227卷,52 - 59页]。结果表明,CMP1和CMP2是酿酒酵母中仅有的编码PP2B催化多肽的基因,并且在正常条件下PP2B活性对于酵母的生长不是必需的。