Reinhard J, Scheel A A, Diekmann D, Hall A, Ruppert C, Bähler M
Friedrich-Miescher Laboratorium der Max-Planck-Gesellschaft, Tübingen, Germany.
EMBO J. 1995 Feb 15;14(4):697-704. doi: 10.1002/j.1460-2075.1995.tb07048.x.
A novel widely expressed type of myosin (fifth unconventional myosin from rat: myr 5) from rat tissues, defining a ninth class of myosins, was identified. The predicted amino acid sequence of myr 5 exhibits several features not found previously in myosins. The myosin head domain contains a unique N-terminal extension and an insertion of 120 amino acids at a postulated myosin-actin contact site. Nevertheless, myr 5 is able to bind actin filaments in an ATP-regulated manner. The head domain is followed by four putative light chain binding sites. The tail domain of myr 5 contains a region which coordinates two atoms of zinc followed by a region that stimulates GTP hydrolysis of members of the ras-related rho subfamily of small G-proteins. Myr 5 therefore provides the first direct link between rho GTPases which have been implicated in the regulation of actin organization and the actin cytoskeleton. It is also the first unconventional myosin for which a tail binding partner(s), namely members of the rho family, has been identified.
从大鼠组织中鉴定出一种新型的广泛表达的肌球蛋白（大鼠的第五种非常规肌球蛋白：myr 5），它定义了第九类肌球蛋白。myr 5的预测氨基酸序列具有一些先前在肌球蛋白中未发现的特征。肌球蛋白头部结构域包含一个独特的N端延伸以及在假定的肌球蛋白-肌动蛋白接触位点处插入的120个氨基酸。尽管如此，myr 5能够以ATP调节的方式结合肌动蛋白丝。头部结构域之后是四个假定的轻链结合位点。myr 5的尾部结构域包含一个能与两个锌原子配位的区域，随后是一个能刺激小G蛋白的ras相关rho亚家族成员的GTP水解的区域。因此，myr 5在与肌动蛋白组织调节有关的rho GTPases和肌动蛋白细胞骨架之间提供了第一个直接联系。它也是第一个已鉴定出尾部结合伴侣（即rho家族成员）的非常规肌球蛋白。
