SMOOTH-MUSCLE CONTRACTILITY IS MODULATED BY MYOSIN TAIL-S2-LMM HINGE REGION INTERACTION
SMOOTH-MUSCLE CONTRACTILITY IS MODULATED BY MYOSIN TAIL-S2-LMM HINGE REGION INTERACTION
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DOI：
10.1152/ajpcell.1995.269.5.c1126
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发表时间：
1995-11-01
影响因子：
5.5
通讯作者：
PAUL, RJ
中科院分区：
文献类型：
--
作者：
CAI, S;FERGUSON, DG;PAUL, RJ
两种主要平滑肌肌球蛋白亚型的功能意义尚不清楚，它们在非酶COOH末端尾区不同。我们在这里报告说，一个13个氨基酸的肽，它模仿了独特的SM 1肌球蛋白亚型的尾巴区域，抑制收缩速度在透化平滑肌。使用十二烷基硫酸钠-聚丙烯酰胺凝胶电泳、光亲和标记和免疫电子显微镜显示该肽与肌球蛋白的S2-轻酶解肌球蛋白（LMM）铰链区结合。我们的研究结果表明，新的分子间接触的尾部和SB-LMM铰链区相邻的肌球蛋白分子在粗丝可以调节收缩性，并提供了一个基础，不同的亚型功能。
The functional significance of two major smooth muscle myosin isoforms, which differ in the nonenzymic COOH-terminal tail region, is not known. We report here that a 13-amino acid peptide, which mimics a region of the tail unique to the SM1 myosin isoform, inhibits contraction velocity in permeabilized smooth muscle. This peptide is shown to bind to the S2-light meromyosin (LMM) hinge region of myosin using sodium dodecyl sulfate-polyacrylamide gel electrophoresis, photoaffinity labeling, and immunoelectron microscopy. Our results suggest that novel intermolecular contacts between the tail and SB-LMM hinge regions of adjacent myosin molecules in the thick filament may modulate contractility and provide a basis for distinct isoform function.