Differential binding of rabbit fast muscle myosin light chain isoenzymes to regulated actin

The direct binding of S1(A1) and S1(A2) to regulated actin has been investigated by centrifugation. Binding was measured in the presence of either Mg·Ado PP[NH] P or Mg·ADP at 24°C at various ionic strengths. At low ionic strength, in either the presence or absence of Ca 2+, the binding of S1(A1) to...

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Veröffentlicht in:	FEBS letters 1985-01, Vol.180 (2), p.170-174
Hauptverfasser:	Trayer, Hylary R., Trayer, Ian P.
Format:	Artikel
Sprache:	eng
Schlagworte:	actin Actin binding Actins - metabolism Adenosine Diphosphate - metabolism Adenylyl Imidodiphosphate - metabolism AdoPP[NH]P, adenosine-5' -[β,gg-imido]triphosphate Analytical, structural and metabolic biochemistry Animals Ap5A,P 1,P 5,P1P5-di(adenosine-5')pentaphosphate Biological and medical sciences Calcium - metabolism Centrifugation Contractile proteins Cooperative binding Fundamental and applied biological sciences. Psychology Holoproteins Isoenzymes - metabolism Magnesium - metabolism muscles Muscles - enzymology myosin Myosin subfragment 1 isoenzyme Myosin Subfragments Myosins - metabolism Osmolar Concentration Peptide Fragments - metabolism Proteins Rabbits Regulated actin S1(A1), S1(A2), rabbit fast-twitch muscle myosin subfragment 1 containing either the alkali 1 (A1 or LC1) light chain or the alkali 2 (A2 or LC2) light chain S1, myosin sub fragment 1 Tn-I, troponin I, the inhibitory component of troponin
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Zusammenfassung:	The direct binding of S1(A1) and S1(A2) to regulated actin has been investigated by centrifugation. Binding was measured in the presence of either Mg·Ado PP[NH] P or Mg·ADP at 24°C at various ionic strengths. At low ionic strength, in either the presence or absence of Ca 2+, the binding of S1(A1) to regulated actin was always stronger than for S1(A2). As the ionic strength was increased the differential binding between S1(A1) and S1(A2) was still maintained in the presence of Ca 2+ but not in its absence. These data are discussed in terms of a modifying role for the N-terminal region of the A1 light chain in regulation of the contractile process.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(85)81065-6