蛋白激酶C与环磷酸腺苷依赖性蛋白激酶之间鱼精蛋白磷酸化位点的比较。
Comparison of phosphorylation sites in protamines between protein kinase C and cAMP-dependent protein kinase.
作者信息
Nishiyama K, Sakai K, Tanaka Y, Kobayashi T, Nakamura S, Sakanoue Y, Hashimoto E, Yamamura H
机构信息
Department of Biology, Kobe University School of Allied Medical Sciences, Japan.
出版信息
Biochem Int. 1988 Jul;17(1):51-8.
Phosphorylation sites of protamines by protein kinase C and cAMP-dependent protein kinase (protein kinase A) were studied. Using clupeine Y1 as a substrate, protein kinase C phosphorylates both Ser and Thr residues, whereas protein kinase A phosphorylates only Ser residue(s). Protein kinase C phosphorylates all Ser and Thr residues of clupeine Y2 and Z, however protein kinase A phosphorylates mainly Ser9 and slightly Thr5 in clupeine Y2 and Ser6 and Ser10 in clupeine Z. These results suggest that protein kinase C recognizes more sites than those of protein kinase A and may participate in protamine phosphorylation in vivo.
研究了蛋白激酶C和环磷酸腺苷依赖性蛋白激酶（蛋白激酶A）对鱼精蛋白的磷酸化位点。以鲱精蛋白Y1作为底物时，蛋白激酶C可使丝氨酸（Ser）和苏氨酸（Thr）残基磷酸化，而蛋白激酶A仅使Ser残基磷酸化。蛋白激酶C可使鲱精蛋白Y2和Z的所有Ser和Thr残基磷酸化，然而蛋白激酶A主要使鲱精蛋白Y2中的Ser9磷酸化且使Thr5轻微磷酸化，使鲱精蛋白Z中的Ser6和Ser10磷酸化。这些结果表明，蛋白激酶C识别的位点比蛋白激酶A更多，并且可能参与体内鱼精蛋白的磷酸化过程。
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