Ca2+ -induced tropomyosin movement in scallop striated muscle thin filaments
Department of Cell Biology
Animals; Calcium; *Microfilaments; Models, Molecular; Muscle Contraction; *Muscle, Skeletal; Pectinidae; Protein Conformation; Tropomyosin; Vertebrates
Striated muscle contraction in most animals is regulated at least in part by the troponin-tropomyosin (Tn-Tm) switch on the thin (actin-containing) filaments. The only group that has been suggested to lack actin-linked regulation is the mollusks, where contraction is regulated through the myosin heads on the thick filaments. However, molluscan gene sequence data suggest the presence of troponin (Tn) components, consistent with actin-linked regulation, and some biochemical and immunological data also support this idea. The presence of actin-linked (in addition to myosin-linked) regulation in mollusks would simplify our general picture of muscle regulation by extending actin-linked regulation to this phylum as well. We have investigated this question structurally by determining the effect of Ca(2+) on the position of Tm in native thin filaments from scallop striated adductor muscle. Three-dimensional reconstructions of negatively stained filaments were determined by electron microscopy and single-particle image analysis. At low Ca(2+), Tm appeared to occupy the "blocking" position, on the outer domain of actin, identified in earlier studies of regulated thin filaments in the low-Ca(2+) state. In this position, Tm would sterically block myosin binding, switching off filament activity. At high Ca(2+), Tm appeared to move toward a position on the inner domain, similar to that induced by Ca(2+) in regulated thin filaments. This Ca(2+)-induced movement of Tm is consistent with the hypothesis that scallop thin filaments are Ca(2+) regulated.
DOI of Published Version
J Mol Biol. 2008 Nov 14;383(3):512-9. Epub 2008 Aug 27. Link to article on publisher's site
Journal of molecular biology
Jung, HyunSuk and Craig, Roger W., "Ca2+ -induced tropomyosin movement in scallop striated muscle thin filaments" (2008). Craig Lab Publications. 8.