Cooperative binding of tropomyosin to actin.
Tropomyosin molecules attach to the thin filament conjointly rather than separately, in a pattern indicating very high cooperativity. The equilibrium process drawing tropomyosins together on the actin filament can be measured by application ofa linear lattice model to bindingisotherm data and hypotheses on the mechanism of cooperativity can be tested. Each end of tropomyosin overlaps and attaches to the end ofa neighboring tropomyosin, facilitating the formation of continuous tropomyosin strands, without gaps between neighboring molecules along the thin filament. Interestingly, the overlap complexes vary greatly in size and composition among tropomyosin isoforms, despite consistently cooperative binding to actin. Also, the tendency of tropomyosin to bind to actin cooperatively rather than randomly does not correlate with the strength ofend-to-end binding.By implication, tropomyosin's actin-binding cooperativity likely involves effects on the actin filament, as well as direct interactions between adjacent tropomyosins.
Tobacman
Larry S
LS
Department of Medicine, University of Illinois at Chicago, Chicago, IL, USA. lst@uic.edu
D008841:Actin Cytoskeleton / Q000737:chemistry; D000199:Actins / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D004305:Dose-Response Relationship, Drug; D017629:Gap Junctions / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D015233:Models, Statistical; D008969:Molecular Sequence Data; D009206:Myocardium / Q000378:metabolism; D011485:Protein Binding; D020033:Protein Isoforms; D017434:Protein Structure, Tertiary; D014335:Tropomyosin / Q000737:chemistry*
D000199:Actins; D020033:Protein Isoforms; D014335:Tropomyosin