Chain register in myosin rod
Chain register in myosin rod
复制标题
肌球蛋白杆中的链寄存器
DOI：
10.1016/0014-5793(82)80896-x
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发表时间：
1982
期刊：
影响因子：
3.5
通讯作者：
M. Stewart
中科院分区：
文献类型：
--
作者：
M. Stewart
肌球蛋白是肌肉和非肌肉细胞收缩机构的重要组成部分。该分子由两个与肌动蛋白相互作用的球状头部和一个长的杆状尾巴组成，在肌肉细胞中，杆状尾巴构成了粗丝的主干。肌球蛋白分子的尾部，通常被称为肌球蛋白棒，可以通过蛋白质分解[L]来制备，它是由两条相同或接近相同的[2]o螺旋链组成的，这些链以盘绕的形式排列[3，4]。通过与对其他纤维收缩蛋白，副肌球蛋白[5]和原肌球蛋白[6-81]的研究相类比，这些链被认为是注册的。然而，这一提议尚未获得确凿的实验证据。现在可以获得大量的肌球蛋白序列信息，为了对其进行分析，了解链的相对位置是至关重要的。在这篇文章中，它证明了在肌球蛋白棒分子的一部分内的链之间可以形成二硫键，这建立了这些链是注册的。
Myosin is an important component of the contractile apparatus of both muscle and non-muscle cells. The molecule consists of two globular heads, which interact with actin, and a long rod-like tail which, in muscle cells, forms the backbone of thick filaments. The tail portion of the myosin molecule, generally referred to as myosin rod, can be prepared by proteolysis [l] and is constructed from two identical or near-identical [2], o-helical chains arranged in a coiledcoil conformation [3, 4]. By analogy with studies on the other fibrous contractile proteins, paramyosin [5] and tropomyosin [6-81, the chains are thought to be in register. However, firm experimental evidence for this proposal has not been obtained. A great deal of myosin sequence information is now becoming available and in order for it to be analysed, it is vital that the relative position of the chains should be known. In this article it is demonstrated that disulphide bonds can be formed between the chains within a portion of the myosin rod molecule, which establishes that these chains are in register.