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J. Biochem, 1976, Vol. 80, No. 2 323-332
© 1976 Japanese Biochemical Society

research-article

{gamma}-Actinin, a New Regulatory Protein from Rabbit Skeletal Muscle II. Action on Actin1

Masaaki KURODA and Koscak MARUYAMA

Department of Biophysics, Faculty of Science, Kyoto University Sakyo-ku, Kyoto, Kyoto 606

The interaction of {gamma};-actinin and actin was investigated under various conditions. It has been shown that {gamma}-actinin affects the G-F transformation of actin, causing an increase in the number of actin monomers required to form a nucleus in the initial step of polymerization. Sonicated fragments of F-actin and heavy meromyosin caused the immediate polymerization of actin under the influence of {gamma}-actinin. Therefore, it can be concluded that {gamma}-actinin inhibits the nucleation step of G-F transformation. Actin filaments which were formed in the presence of {gamma}-actinin (F*-actin) were shown to possess certain characteristic properties when compared with control F-actin. These were as follows: F*-actin solution had a high critical concentration; F*-actin showed a high rate of depolymerization; the flow birefringence of F*-actin decreased with time upon incubation in the absence of free ATP; finally, F*-actin was demonstrated to have ATP-splitting activity. These dynamic features of F*-actin were accounted for in terms of an increase in the rate constant of depolymerization in F*-actin under the influence of {gamma}-actinin.

1 This work was supported by grants from the Ministry of Education, Science and Culture, of Japan, and from the Muscular Dystrophy Associations of America, Inc.


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