A NOVEL MYOSIN-I FROM BOVINE ADRENAL-GLAND

被引：21

作者：

ZHU, T ^{[1
]}

IKEBE, M ^{[1
]}

机构：

[1] CASE WESTERN RESERVE UNIV,SCH MED,DEPT PHYSIOL & BIOPHYS,CLEVELAND,OH 44106

来源：

FEBS LETTERS | 1994年 / 339卷 / 1-2期

关键词：

MYOSIN I; PRIMARY STRUCTURE; MOLECULAR CLONING; ADRENAL GLAND;

D O I：

10.1016/0014-5793(94)80378-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 Ca2+-independent calmodulin binding consensus sequence, suggesting that the novel myosin I binds calmodulin. This was confirmed by calmodulin overlay which showed the binding of I-125-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.

引用

页码：31 / 36

页数：6

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