PMID: 11606251Oct 19, 2001Paper

C-terminal actin-binding sites of smooth muscle caldesmon switch actin between conformational states

The International Journal of Biochemistry & Cell Biology
Y S BorovikovS B Marston

Abstract

Caldesmon is a component of the thin filaments of smooth muscles where it is believed to play an essential role in regulating the thin filaments' interaction with myosin and hence contractility. We studied the effects of caldesmon and two recombinant fragments CaDH1 (residues 506-793) and CaDH2 (residues 683-767) on the structure of actin-tropomyosin by making measurements of the fluorescence polarisation of probes specifically attached to actin. CaDH1, like the parent molecule caldesmon, is an inhibitor of actin-tropomyosin interaction with myosin whilst CaDH2 is an activator. The F-actin in permeabilised and myosin free rabbit skeletal muscle 'ghost' fibres was labelled by tetramethyl rhodamine-isothiocyanate (TRITC)-phalloidin or fluorescein-5'-isothiocyanate (FITC) at lysine 61. Fluorescence polarisation measurements were made and the parameters Phi(A), Phi(E), Theta(1/2) and Nu were calculated. Phi(A) and Phi(E) are angles between the fiber axis and the absorption and emission dipoles, respectively; Theta(1/2) is the angle between the F-actin filament axis and the fiber axis; Nu is the relative number of randomly oriented fluorophores. Actin-tropomyosin interaction with myosin subfragment-1 induced changes in the parameter...Continue Reading

References

Dec 21, 1989·Biochimica Et Biophysica Acta·E NowakR Dabrowska
Jul 7, 1986·FEBS Letters·A Szpacenko, R Dabrowska
Dec 18, 1987·Biochimica Et Biophysica Acta·B GałazkiewiczR Dabrowska
Aug 25, 1995·The Journal of Biological Chemistry·I D Fraser, S B Marston
Feb 4, 1999·Pflügers Archiv : European journal of physiology·D J Burton, S B Marston

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