Negron J A, Gonzalez S, Rodriguez-Medina J R
Department of Biochemistry, University of Puerto Rico, San Juan 00936.
Biochem Biophys Res Commun. 1996 Apr 25;221(3):515-20. doi: 10.1006/bbrc.1996.0628.
Phosphorylation of the myosin heavy chain has been shown to be a key regulatory mechanism of several non-muscle myosins. In this study we present evidence demonstrating that the yeast type II myosin heavy chain is phosphorylated in vivo. Phosphorylation of serine residues was confirmed by direct metabolic labeling with [32P] and by indirect immunostaining of phosphoserine with a specific monoclonal antibody. Loss of immunoreactivity in a targeted deletion of the 26 amino acid carboxyl terminal segment of the type II myosin heavy chain suggests that the phosphorylation occurs at one or more serine residues located between residues 1903 and 1928.
肌球蛋白重链的磷酸化已被证明是几种非肌肉肌球蛋白的关键调节机制。在本研究中，我们提供证据表明酵母II型肌球蛋白重链在体内发生磷酸化。通过用[32P]进行直接代谢标记以及用特异性单克隆抗体对磷酸丝氨酸进行间接免疫染色，证实了丝氨酸残基的磷酸化。II型肌球蛋白重链26个氨基酸羧基末端片段的靶向缺失导致免疫反应性丧失，这表明磷酸化发生在1903和1928位残基之间的一个或多个丝氨酸残基上。
