PHOSPHORYLATABLE SERINE RESIDUES ARE LOCATED IN A NON-HELICAL TAILPIECE OF A CATCH MUSCLE MYOSIN
PHOSPHORYLATABLE SERINE RESIDUES ARE LOCATED IN A NON-HELICAL TAILPIECE OF A CATCH MUSCLE MYOSIN
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DOI：
10.1007/bf01738758
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发表时间：
1988-12-01
影响因子：
2.7
通讯作者：
COHEN, C
中科院分区：
文献类型：
--
作者：
CASTELLANI, L;ELLIOTT, BW;COHEN, C
来自软体动物捕获肌肉的肌球蛋白显示出不寻常的性质：当在杆中被内源性重链激酶磷酸化时，肌球蛋白溶解度增强并且分子折叠（Castellani和Cohen，Proc. natn. Acad. Sci. U.S.A.84，（1987）4058-62）。我们现在已经通过选择性蛋白水解切割将磷酸化位点定位于杆的羧基末端。两个主要的延伸序列，18和21个残基长，已被确定，每个含有一个磷酸丝氨酸残基。对这两种肽的氨基酸序列的分析表明它们形成非螺旋尾片段。我们讨论了如何磷酸化这个尾片段可能会影响酶的活性在捕捉肌肉粗丝。
Myosin from a molluscan catch muscle displays unusual properties: when phosphorylated in the rod by an endogenous heavy-chain kinase, myosin solubility is enhanced and the molecule folds (Castellani and Cohen, Proc. natn. Acad. Sci. U.S.A. 84, (1987) 4058-62). We have now localized the sites of phosphorylation to the carboxy-terminal end of the rod by selective proteolytic cleavage. Two major stretches of sequence, 18 and 21 residues long, have been identified, each containing a single residue of phosphoserine. Analysis of the amino-acid sequence of these two peptides indicates that they form a non-helical tailpiece. We discuss how phosphorylation of this tailpiece might influence enzymatic activity in catch muscle thick filaments.