MacKintosh R W, Haycox G, Hardie D G, Cohen P T
Department of Biochemistry, University of Dundee, Scotland, UK.
FEBS Lett. 1990 Dec 10;276(1-2):156-60. doi: 10.1016/0014-5793(90)80531-m.
Two clones encoding protein phosphatase (PP) catalytic subunits have been isolated from a Brassica napus cDNA library screened with rabbit muscle PP1 alpha and PP2A alpha cDNAs. The deduced protein sequences are very similar to those of mammalian PP1 alpha and PP2A alpha (72% and 79% overall identity, respectively) indicating that they are the plant homologues of PP1 alpha and PP2A alpha. This high degree of similarity provides a molecular explanation for the remarkable conservation of the catalytic and regulatory properties between animal and plant protein phosphatases and supports the concept that PP1 and PP2A may be the most highly conserved of known enzymes.
用兔肌肉PP1α和PP2Aα cDNA筛选甘蓝型油菜cDNA文库,分离出两个编码蛋白磷酸酶(PP)催化亚基的克隆。推导的蛋白质序列与哺乳动物PP1α和PP2Aα的序列非常相似(总体一致性分别为72%和79%),表明它们是PP1α和PP2Aα的植物同源物。这种高度相似性为动植物蛋白磷酸酶之间催化和调节特性的显著保守性提供了分子解释,并支持了PP1和PP2A可能是已知酶中最保守的这一概念。