Troponin I and caldesmon restrict alterations in actin structure occurring on binding of myosin subfragment I

FEBS Letters

Dabrowska, Renata²  Khoroshev, Mikhail I.¹  Nowak, Ewa²  Borovikov, Yurii S.¹ 

[1] Cell Motility Group, Institute of Cytology of the Academy of Sciences of USSR, Leningrad, USSR;Department of Muscle Biochemistry, Nencki Institute of Experimental Biology, Warsaw, Poland

关键词: Troponin I;    Caldesmon;    Actin dynamics;    Actin-myosin interaction;    Polarized fluorescence;   

DOI  :  10.1016/0014-5793(91)80356-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown