Replacement of threonine residues by serine and alanine in a phosphorylatable heavy chain fragment of Dictyostelium myosin II

FEBS Letters

Schleicher, Michael¹  Grabatin, Barbara¹  Lück-Vielmetter, Dorothea¹  Wippler, Jürgen¹  Gerisch, Günther¹ 

[1] Max-Planck-Institut für Biochemie, 8033 Martinsried, FRG

关键词: Cell motility;    Chemotaxis;    Dictyostelium discoideum;    Myosin phosphorylation;    DTT;    dithiothreitol;    kinaseagg;    soluble myosin heavy chain kinase from aggregation competent cells of Dictyostelium discoideum;    kinasegrw;    soluble myosin heavy chain kinase from growth phase cells;    MHC;    myosin heavy chain;    SDS;    sodium dodecyl sulfate;   

DOI  :  10.1016/0014-5793(90)81163-I

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown