Effect of actin C-terminal modification on tropomyosin isoforms binding and thin filament regulation

被引:18
|
作者
Skorzewski, Radoslaw [1 ]
Sliwinska, Malgorzata [1 ]
Borys, Danuta [1 ]
Sobieszek, Apolinary [2 ]
Moraczewska, Joanna [1 ]
机构
[1] Kazimierz Wielki Univ Bydgoszcz, Dept Expt Biol, PL-85064 Bydgoszcz, Poland
[2] Austrian Acad Sci, Life Sci Ctr, Inst Biomed Aging Res, A-6020 Innsbruck, Austria
来源
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS | 2009年 / 1794卷 / 02期
基金
英国惠康基金;
关键词
Actin; Truncated actin; Tropomyosin; Smooth muscle; Non-muscle; Regulation; RABBIT SKELETAL-MUSCLE; MYOSIN SUBFRAGMENT 1; F-ACTIN; YEAST ACTIN; TROPONIN; ACTIVATION; RESIDUES; SMOOTH; COMPLEX; ATPASE;
D O I
10.1016/j.bbapap.2008.10.014
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
Tropomyosins, a family of actin-binding regulatory proteins, are present in muscle and non-muscle cells. Multiple tropomyosin (TM) isoforms differ in actin affinity and regulatory properties, but little is known about the molecular bases of these differences. The C-terminus of actin stabilizes contacts between actin subunits in the filament and interacts with myosin and regulatory proteins. The goal of this work was to reveal how structural changes in actin and differences between TM isoforms affect binding between these proteins and affect thin filament regulation. Actin proteolytically truncated by three C-terminal amino acids exhibited 1.2-1.5 fold reduced affinity for non-muscle and smooth muscle tropomyosin isoforms. The truncation increased the cooperativity of myosin S1-induced tropomyosin binding for short tropomyosins (TM5a and TM1b9a), but it was neutral for long isoforms (smTM and TM2). Actin modification affected regulation of actomyosin ATPase activity in the presence of all tropomyosins by shifting the filament into a more active state. We conclude that the integrity of the actin C-terminus is important for actin-tropomyosin interactions, however the increased affinity of tropomyosin binding in the S1-induced state of the filament appears not to be involved in the tropomyrosin isoform-dependent mechanism of the actomyosin ATPase activation. (C) 2008 Elsevier B.V. All rights reserved.
引用
收藏
页码:237 / 243
页数:7
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