Evidence that the head of kinesin is sufficient for force generation and motility in vitro.
Evidence that the head of kinesin is sufficient for force generation and motility in vitro.
复制标题
有证据表明驱动蛋白的头部足以在体外产生力和运动。
DOI：
10.1126/science.2142332
复制
发表时间：
1990
期刊：
影响因子：
--
通讯作者：
Goldstein,LS
中科院分区：
文献类型：
--
作者：
Yang,JT;Saxton,WM;Stewart,RJ;Raff,EC;Goldstein,LS
驱动蛋白是一种机械化学蛋白质，其将三磷酸腺苷中的化学能转化为机械力以使细胞组分沿沿着运动。通过研究在大肠杆菌中表达的Drosophilakinesin重链及其截短形式，确定了驱动蛋白分子中负责产生运动的区域。结果表明，（i）驱动蛋白重链单独，没有轻链和其他真核细胞因子，能够诱导微管运动在体外，和（ii）可能只包含驱动蛋白头部的片段也能够诱导微管运动。因此，驱动蛋白氨基末端的450个氨基酸含有将化学能转化为机械力所需的所有基本元素。
Kinesin is a mechanochemical protein that converts the chemical energy in adenosine triphosphate into mechanical force for movement of cellular components along microtubules. The regions of the kinesin molecule responsible for generating movement were determined by studying the heavy chain ofDrosophilakinesin, and its truncated forms, expressed inEscherichia coli. The results demonstrate that (i) kinesin heavy chain alone, without the light chains and other eukaryotic factors, is able to induce microtubule movement in vitro, and (ii) a fragment likely to contain only the kinesin head is also capable of inducing microtubule motility. Thus, the amino-terminal 450 amino acids of kinesin contain all the basic elements needed to convert chemical energy into mechanical force.