REPLACEMENT OF THREONINE RESIDUES BY SERINE AND ALANINE IN A PHOSPHORYLATABLE HEAVY-CHAIN FRAGMENT OF DICTYOSTELIUM MYOSIN-II

被引:75
作者
LUCKVIELMETTER, D [1 ]
SCHLEICHER, M [1 ]
GRABATIN, B [1 ]
WIPPLER, J [1 ]
GERISCH, G [1 ]
机构
[1] MAX PLANCK INST BIOCHEM,W-8033 MARTINSRIED,GERMANY
关键词
Cell motility; Chemotaxis; Dictyostelium discoideum; Myosin phosphorylation;
D O I
10.1016/0014-5793(90)81163-I
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The target sites of soluble myosin heavy chain kinases partially purified from growth phase or aggregation competent cells of Dictyostelium discoideum were identified by the use of normal and mutated fragments of the myosin heavy chain. The kinases from both developmental stages phosphorylated two previously established threonine residues, as well as an additional one. The newly identified site is located within the putative core region of the coiled-coil formed by the myosin tail. A lysine following the phosphorylated threonine residue is the only common feature of the sequences around these sites. The kinases, which specifically phosphorylate threonine residues in wild-type myosin, did accept serine if it was in the right structural context. © 1990.
引用
收藏
页码:239 / 243
页数:5
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