[Phosphorylation of light chains of myosin from rabbit skeletal muscles affects the type of conformation changes of F-actin induced by heavy meromyosin].
The changes in F-actin conformation in myosin-free single ghost fiber induced by the binding of heavy meromyosin (HMM) with dephosphorylated or phosphorylated light chains-2 (LC2) have been studied by measuring intrinsic tryptophan polarized fluorescence of F-actin. It has been found that at low concentrations of Ca2+ (pCa greater than or equal to 8), the binding of HMM with dephosphorylated LC2 to F-actin in ghost fibres increases, whereas the binding of HMM with phosphorylated LC2 decreases the anisotropy of polarized tryptophan fluorescence. The effect is reversed at high concentrations of Ca2+ (pCa = 5). It has been assumed that this effect of myosin light chains phosphorylation may be due to its influence on the type of myosin head binding to F-actin.
D000199:Actins / Q000378:metabolism*; D000818:Animals; D005456:Fluorescent Dyes; D066298:In Vitro Techniques; D008970:Molecular Weight; D009132:Muscles / Q000378:metabolism*; D015879:Myosin Subfragments / Q000378:metabolism*; D009219:Myosin-Light-Chain Kinase; D009218:Myosins / Q000378:metabolism*; D010766:Phosphorylation; D011487:Protein Conformation; D011494:Protein Kinases / Q000378:metabolism; D011817:Rabbits
D000199:Actins; D005456:Fluorescent Dyes; D015879:Myosin Subfragments; D011494:Protein Kinases; D009219:Myosin-Light-Chain Kinase; D009218:Myosins
Fosforilirovanie legkikh tsepeĭ miozina iz skeletnykh myshts krolika vliiaet na kharakter konformatsionnykh izmeneniĭ F-aktina, indutsiruemykh tiazhelym meromiozinom.