Ohtsuki K, Nishikawa Y, Saito H, Munakata H, Kato T
Laboratory of Genetical Biochemistry, Kitasato University School of Allied Health Sciences, Sagamihara, Japan.
FEBS Lett. 1996 Jan 8;378(2):115-20. doi: 10.1016/0014-5793(95)01424-1.
The stimulatory effect of DNA-binding sperm proteins (histone and protamine) on the phosphorylation of p98 (ERp99/GRp94, one of the Hsp-90 family of proteins) by egg casein kinase II (CK-II) was investigated in vitro. It was found that (i) phosphorylation of p98 by egg CK-II in vitro is greatly stimulated by poly-Arg, but not by poly-Lys; and (ii) similar stimulation is observed with sperm histones H2B2 and H2B3 (sea urchin) and fish protamines, such as salmine A1 (salmon) and protamine 3a (rainbow trout). These findings suggest that these DNA-binding sperm proteins function as potent activators for CK-II in fertilized eggs. All of these DNA-binding sperm proteins contain at least an oligo-Arg cluster as a common feature, which can interact with an acidic amino acid cluster of the regulatory beta-subunit CK-II.
在体外研究了DNA结合精子蛋白(组蛋白和鱼精蛋白)对卵酪蛋白激酶II(CK-II)磷酸化p98(ERp99/GRp94,热休克蛋白90家族蛋白之一)的刺激作用。发现:(i)卵CK-II在体外对p98的磷酸化受到聚精氨酸的极大刺激,但不受聚赖氨酸的刺激;(ii)在精子组蛋白H2B2和H2B3(海胆)以及鱼类鱼精蛋白如鲑精蛋白A1(鲑鱼)和鱼精蛋白3a(虹鳟鱼)中观察到类似的刺激作用。这些发现表明,这些DNA结合精子蛋白在受精卵中作为CK-II的有效激活剂发挥作用。所有这些DNA结合精子蛋白都至少含有一个寡聚精氨酸簇作为共同特征,该簇可与调节性β亚基CK-II的酸性氨基酸簇相互作用。