INTERFERENCE WITH MYOSIN SUBFRAGMENT-1 BINDING BY SITE-DIRECTED MUTAGENESIS OF ACTIN

被引：55

作者：

ASPENSTROM, P ^{[1
]}

KARLSSON, R ^{[1
]}

机构：

[1] UNIV UPPSALA,CTR BIOMED,DEPT DEV BIOL,BOX 587,S-75123 UPPSALA,SWEDEN

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1991年 / 200卷 / 01期

关键词：

D O I：

10.1111/j.1432-1033.1991.tb21045.x

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：

Three N-terminal double mutants of beta-actin expressed in the yeast Saccharomyces cerevisiae have been characterized with respect to DNase-I interaction, N-terminal post-translational modification, polymerizability and myosin subfragment-1 binding. The results strongly support earlier suggestions that the acidic residues at the N-terminus of actin are part of the myosin-binding site, while they seem to be of no importance for the other aspects of actin biochemistry tested. The suitability of this expression system for production of recombinant actin in general is discussed.

引用

页码：35 / 41

页数：7

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