Premium
Troponin I and caldesmon restrict alterations in actin structure occurring on binding of myosin subfragment I
Author(s) -
Nowak Ewa,
Borovikov Yurii S.,
Khoroshev Mikhail I.,
Dabrowska Renata
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80356-8
Subject(s) - caldesmon , myosin , actin , biophysics , tropomyosin , troponin , chemistry , actina , myosin light chain kinase , biochemistry , microbiology and biotechnology , biology , cytoskeleton , medicine , calmodulin , enzyme , myocardial infarction , cell
The effect of troponin I and caldesmon on phalloidin‐rhodamine‐ and 1,5‐IAEDANS‐labelled actin in skeletal muscle ghost fibers was investigated by polarized fluorescence. Both these proteins inhibited the structural alterations in the actin monomer and the increase of flexibility of actin filaments occurring on binding of myosin heads, and their effects were potentiated by tropomyosin. This immobilization of the actin filament through troponin I and caldesmon seems to originate from restriction of the relative motions of the two domains within the monomer.