Lees-Miller S P, Anderson C W
Biology Department, Brookhaven National Laboratory, Upton, New York 11973.
J Biol Chem. 1989 Oct 15;264(29):17275-80.
The 90-kDa heat-shock protein, hsp90, is an abundant cytoplasmic protein that can be phosphorylated in vitro by a double-stranded (ds) DNA-activated protein kinase found in cells from several species. Here we show that the dsDNA-activated protein kinase from human HeLa cells phosphorylates 2 threonine residues in the sequence PEETQTQDQPME at the amino terminus of human hsp90 alpha. Hsp90 beta, which is 97% identical to hsp90 alpha but lacks both amino-terminal threonines, is not phosphorylated by the dsDNA-activated protein kinase. Mouse hsp86 and rabbit hsp90 alpha are homologous to human hsp90 alpha; both heterologous proteins are phosphorylated at the same amino-terminal threonines by the human dsDNA-activated protein kinase.
90千道尔顿热休克蛋白（hsp90）是一种丰富的细胞质蛋白，在体外可被几种物种细胞中发现的双链（ds）DNA激活的蛋白激酶磷酸化。在此我们表明，来自人HeLa细胞的dsDNA激活的蛋白激酶可使人hsp90α氨基末端序列PEETQTQDQPME中的2个苏氨酸残基磷酸化。hsp90β与hsp90α有97%的同源性，但缺乏氨基末端的苏氨酸，不能被dsDNA激活的蛋白激酶磷酸化。小鼠hsp86和兔hsp90α与人hsp90α同源；这两种异源蛋白均可被人dsDNA激活的蛋白激酶在相同的氨基末端苏氨酸处磷酸化。
