[The effect of proteolysis of myosin heads on conformational changes induced by them in F-actin].
The effect of limited proteolysis of myosin subfragment I (S1) on conformational changes in F-actin during the formation of a rigor F-actin-S1 complex was studied, using polarized microfluorimetry. Upon the decoration of thin filaments made up of rhodaminyl-phalloin modified F-actin with subfragment I, the anisotropy of fluorescence increased. Limited proteolysis of S1 at the junctions of 27 kD-70 kD and 27 kD-50 kD-20 kD fragments as well as the destruction of the 50 kD fragment by methanol had no effect on the nature of these changes. It was assumed that during the formation of the actomyosin complex the conformational changes in F-actin were induced by the 20 kD fragment. The 27 kD and 50 kD fragments seemed to exert a weak influence on action conformation within the complex.
Borovikov
Iu S
IuS
Kuleva
N V
NV
Khoroshev
M I
MI
Vdovina
I B
IB
D000199:Actins / Q000378:metabolism*; D000818:Animals; D017301:Ca(2+) Mg(2+)-ATPase / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D009132:Muscles / Q000201:enzymology / Q000378:metabolism; D015879:Myosin Subfragments; D009218:Myosins / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism*; D010447:Peptide Hydrolases; D011487:Protein Conformation; D011817:Rabbits
D000199:Actins; D015879:Myosin Subfragments; D010446:Peptide Fragments; D010447:Peptide Hydrolases; D017301:Ca(2+) Mg(2+)-ATPase; D009218:Myosins
Vliianie proteoliza miozinovykh golovok na indutsiruemye imi strukturnye perestroĭki F-aktina.