Cofilin-induced cooperative conformational changes of actin subunits revealed using cofilin-actin fusion protein.

ABSTRACT: To investigate cooperative conformational changes of actin filaments induced by cofilin binding, we engineered a fusion protein made of Dictyostelium cofilin and actin. The filaments of the fusion protein were functionally similar to actin filaments bound with cofilin in that they did not bind rhodamine-phalloidin, had quenched fluorescence of pyrene attached to Cys374 and showed enhanced susceptibility of the DNase loop to cleavage by subtilisin. Quantitative analyses of copolymers made of different ratios of the fusion protein and control actin further demonstrated that the fusion protein affects the structure of multiple neighboring actin subunits in copolymers. Based on these and other recent related studies, we propose a mechanism by which conformational changes induced by cofilin bin

SUBMITTER: Umeki N 

PROVIDER: S-EPMC4740740 | biostudies-literature | 2016 Feb

REPOSITORIES: biostudies-literature