Sneddon A A, Cohen P T, Stark M J
Department of Biochemistry, The University, Dundee, UK.
EMBO J. 1990 Dec;9(13):4339-46. doi: 10.1002/j.1460-2075.1990.tb07883.x.
Two genes (PPH21 and PPH22) encoding the yeast homologues of protein serine-threonine phosphatase 2A have been cloned from a Saccharomyces cerevisiae genomic library using a rabbit protein phosphatase 2A cDNA as a hybridization probe. The PPH genes are genetically linked on chromosome IV and are predicted to encode polypeptides each with 74% amino acid sequence identity to rabbit type 2A protein phosphatase, indicating once again the extraordinarily high degree of sequence conservation shown by protein-phosphatases from different species. The two PPH genes show less than 10% amino acid sequence divergence from each other and while disruption of either PPH gene alone is without any major effect, the double disruption is lethal. This indicates that protein phosphatase 2A activity is an essential cellular function in yeast. Measurement of type 2A protein phosphatase activity in yeast strains lacking one or other of the genes indicates that they account for most, if not all, protein phosphatase 2A activity in the cell.
利用兔蛋白磷酸酶2A的cDNA作为杂交探针,已从酿酒酵母基因组文库中克隆出两个编码蛋白丝氨酸 - 苏氨酸磷酸酶2A酵母同源物的基因(PPH21和PPH22)。PPH基因在第四条染色体上呈遗传连锁,预计它们编码的多肽与兔2A型蛋白磷酸酶的氨基酸序列一致性均为74%,这再次表明不同物种的蛋白磷酸酶具有极高的序列保守程度。这两个PPH基因彼此间的氨基酸序列差异小于10%,单独破坏任一PPH基因没有任何重大影响,但双基因破坏是致死的。这表明蛋白磷酸酶2A的活性是酵母细胞中的一项基本功能。在缺失其中一个基因的酵母菌株中对2A型蛋白磷酸酶活性的测量表明,它们即便不能代表细胞中全部的蛋白磷酸酶2A活性,也占了大部分。