Difference in polymerization and steady-state dynamics of free and gelsolin-capped filaments formed by alpha- and beta-isoactins.
The polymerization of scallop beta-like actin is significantly slower than that of skeletal muscle alpha-actin. To reveal which steps of polymerization contribute to this difference, we estimated the efficiency of nucleation of the two actins, the rates of filament elongation at spontaneous and gelsolin-nucleated polymerization and the turnover rates of the filament subunits at steady-state. Scallop actin nucleated nearly twice less efficient than rabbit actin. In actin filaments with free ends, when dynamics at the barbed ends overrides that at the pointed ends, the relative association rate constants of alpha- and beta-actin were similar, whereas the relative dissociation rate constant of beta-ATP-actin subunits was 2- to 3-fold higher than that of alpha-actin. The 2- to 3-fold faster polymerization of skeletal muscle versus scallop Ca-actin was preserved with gelsolin-capped actin filaments when only polymerization at the pointed end is possible. With gelsolin-induced polymerization, the rate constants of dissociation of ATP-actin subunits from the pointed ends were similar, while the association rate constant of beta-actin to the pointed filament ends was twice lower than that of alpha-actin. This difference may be of physiological relevance for functional intracellular sorting of actin isoforms.
Khaitlina
Sofia
S
Institute of Cytology, Russian Academy of Sciences, Cell Culture Department, Tykhoretski Avenue 4, 194064 Sankt-Petersburg, Russia. skhspb@yahoo.com
Hinssen
Horst
H
D000199:Actins / Q000737:chemistry*; D000818:Animals; D001665:Binding Sites; D003198:Computer Simulation; D019281:Dimerization; D018260:Gelsolin / Q000737:chemistry*; D007700:Kinetics; D008956:Models, Chemical; D046912:Multiprotein Complexes / Q000737:chemistry; D049897:Pectinidae; D011485:Protein Binding; D011817:Rabbits
D000199:Actins; D018260:Gelsolin; D046912:Multiprotein Complexes