CHARGE-REVERSION MUTAGENESIS OF DICTYOSTELIUM ACTIN TO MAP THE SURFACE RECOGNIZED BY MYOSIN DURING ATP-DRIVEN SLIDING MOTION

被引：82

作者：

JOHARA, M

TOYOSHIMA, YY

ISHIJIMA, A

KOJIMA, H

YANAGIDA, T

SUTOH, K

机构：

[1] OCHANOMIZU UNIV,FAC SCI,DEPT BIOL,TOKYO 112,JAPAN

[2] OSAKA UNIV,DEPT BIOPHYS ENGN & SCI,TOYONAKA,OSAKA 560,JAPAN

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1993年 / 90卷 / 06期

关键词：

SITE-DIRECTED MUTAGENESIS; INVITRO MOTILITY ASSAY; FORCE GENERATION; ACTIN-ACTIVATED MYOSIN ATPASE;

D O I：

10.1073/pnas.90.6.2127

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Amino acid residues D24/D25, E99/E100, E360/E361, and D363/E364 in subdomain 1 of Dictyostelium actin were replaced with histidine residues by site-directed mutagenesis. Mutant actins were expressed in Dictyostelium cells and purified to homogeneity. The sliding movement of mutant actin filaments on heavy meromyosin attached to a glass surface was measured to assess the effect of the mutation on the motility of actin. For two C-terminal mutants, force generated by a single actin filament and myosin was also measured. These measurements indicated that both D24/D25 and E99/E100 are involved in ATP-driven sliding, whereas E360/E361/D363/E364 are not essential for ATP-driven sliding and force generation.

引用

页码：2127 / 2131

页数：5

共 32 条

[1] SITE-SPECIFIC AMINO-TERMINAL MUTANTS OF YEAST-EXPRESSED BETA-ACTIN - CHARACTERIZATION OF THE INTERACTION WITH MYOSIN AND TROPOMYOSIN [J].