一种来自牛肾上腺的新型肌球蛋白I。

A novel myosin I from bovine adrenal gland.

作者信息

Zhu T, Ikebe M

机构信息

Department of Physiology and Biophysics, School of Medicine, Case Western Reserve University, Cleveland, OH 44106.

出版信息

FEBS Lett. 1994 Feb 14;339(1-2):31-6. doi: 10.1016/0014-5793(94)80378-1.

DOI:10.1016/0014-5793(94)80378-1

PMID:8313976

Abstract

A 3.5 kb cDNA clone was isolated from bovine adrenal gland cDNA library. The clone contained a full-length 3.1 kb open reading frame, encoding a novel myosin I. The deduced amino acid sequence was highly homologous to other known myosin Is in the N-terminal 2 kb region which corresponds to the myosin head domain, while no strong homology was detected in the tail region. The head-tail junction contained the Ca(2+)-independent calmodulin binding consensus sequence, suggesting that the novel myosin I binds calmodulin. This was confirmed by calmodulin overlay which showed the binding of 125I-calmodulin to the recombinant myosin I expressed in E. coli. Northern blots with probes from head and tail regions of this myosin I revealed that this novel myosin I is widely distributed among various tissues.

摘要

从牛肾上腺cDNA文库中分离出一个3.5 kb的cDNA克隆。该克隆包含一个全长3.1 kb的开放阅读框，编码一种新型肌球蛋白I。推导的氨基酸序列在对应于肌球蛋白头部结构域的N端2 kb区域与其他已知的肌球蛋白I高度同源，而在尾部区域未检测到强同源性。头尾连接处含有不依赖Ca(2+)的钙调蛋白结合共有序列，表明这种新型肌球蛋白I与钙调蛋白结合。钙调蛋白覆盖实验证实了这一点，该实验显示125I-钙调蛋白与在大肠杆菌中表达的重组肌球蛋白I结合。用该肌球蛋白I头部和尾部区域的探针进行Northern印迹分析表明，这种新型肌球蛋白I广泛分布于各种组织中。