ACTIN AND THE ACTOMYOSIN INTERFACE - A REVIEW

被引:54
作者
DOSREMEDIOS, CG
MOENS, PDJ
机构
[1] Muscle Research Unit, Department of Anatomy and Histology, The University of Sydney, Sydney
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 1995年 / 1228卷 / 2-3期
基金
英国医学研究理事会;
关键词
ACTIN; ACTOMYOSIN INTERFACE;
D O I
10.1016/0005-2728(94)00169-6
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
This review deals with the structure of the actin monomer, its assembly into filaments and the loci on F-actin involved in binding myosin. Two distinctly different arrangements of monomers have been suggested for actin filaments. One model proposed by Holmes et al, is well developed. It places the so-called 'large' domain close to the filament axis and the so-called 'small' domain out near the surface of the filament. A second, less-well developed, model proposed by Schutt et al. locates the 'small' domain close to the filament axis and they rotate the monomer so that 'bottom' of the 'large' domain is at the highest radius. We analyze the available evidence for the models of F-actin derived from X-ray diffraction, reconstructions from electron micrographs, fluorescence resonance energy transfer spectroscopy, chemical crosslinking, antibody probes, limited proteolysis, site-directed and natural mutations, nuclear magnetic resonance spectroscopy and other techniques. The result is an actin-centered view of the loci on actin which are probably involved in its interaction with the myosin 'head'. From these multiple contacts we speculate on the sequence of steps between the initial weak-binding state of S-1 to the actin filament through to the stable strong-binding state seen in the absence of free Mg-ATP, i.e., the rigor state.
引用
收藏
页码:99 / 124
页数:26
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