Abstract
Changes in the phosphorylation of nonhistone chromosomal proteins have been followed in rat uterus stimulated by 17β-estradiol. Isolated uteri were found to incorporate 32P i into nonhistone proteins via an endogenous nuclear protein kinase reaction. The rate of 32P labeling of nonhistone proteins and the activity of nuclear protein kinase(s) were found to be elevated over three- and two-fold respectively in uteri obtained from ovariectomized animals treated with estrogen. A dramatic change was observed in the radioactivity profile of 32P-labeled proteins fractionated via sodium dodecyl sulfate-polyacrylamide gel electrophoresis. These observations are compatable with the hypothesis that phosphorylation of nonhistone proteins plays a role in the regulation of gene activity in the uterus.
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