[Tropomyosin and myosin subfragment 1 induce in thin muscle fiber filaments differing conformational changes in the C-terminal portion of the polypeptide chain of actin].
Muscle fibres, free of myosin, troponin and tropomyosin, containing thin filaments reconstructed from G-actin and modified by fluorescent label 1,5-IAEDANS were used for polarized microfluorimetric studies of the effect of tropomyosin (TM) from smooth muscles, and of subfragment 1 (S1) from skeletal muscles on the structural state of F-actin. TM and S1 were shown to initiate different changes in polarized fluorescence of 1,5-IAEDANS of F-actin: TM increases, whereas S1 decreases fluorescent anisotropy. It was suggested that the structural state of F-actin may differ in the C-terminal of polypeptide chain of actin.
Borovikov
Iu S
IuS
Dobrowolski
Z
Z
Dabrowska
R
R
D008841:Actin Cytoskeleton / Q000187:drug effects* / Q000648:ultrastructure; D000199:Actins / Q000032:analysis*; D000818:Animals; D003599:Cytoskeleton / Q000187:drug effects*; D005434:Flow Cytometry / Q000379:methods; D005456:Fluorescent Dyes; D066298:In Vitro Techniques; D009130:Muscle, Smooth / Q000187:drug effects* / Q000648:ultrastructure; D015879:Myosin Subfragments; D009218:Myosins / Q000494:pharmacology*; D009282:Naphthalenesulfonates; D010443:Peptide Chain Termination, Translational / Q000187:drug effects*; D010446:Peptide Fragments / Q000494:pharmacology*; D010455:Peptides / Q000032:analysis*; D011487:Protein Conformation / Q000187:drug effects; D011817:Rabbits; D014335:Tropomyosin / Q000494:pharmacology*
D000199:Actins; D005456:Fluorescent Dyes; D015879:Myosin Subfragments; D009282:Naphthalenesulfonates; D010446:Peptide Fragments; D010455:Peptides; D014335:Tropomyosin; C006421:1,5-I-AEDANS; D009218:Myosins
Tropomiozin i subfragment-1 miozina indutsiruiut v tonkikh nitiakh myshechnogo volokna raznye po kharakteru konformatsionnye perestroĭki C-kontsevogo uchastka polipeptidnoĭ tsepi aktina.