Charge-reversion mutagenesis of Dictyostelium actin to map the surface recognized by myosin during ATP-driven sliding motion.
AUTOR(ES)
Johara, M
RESUMO
Amino acid residues D24/D25, E99/E100, E360/E361, and D363/E364 in subdomain 1 of Dictyostelium actin were replaced with histidine residues by site-directed mutagenesis. Mutant actins were expressed in Dictyostelium cells and purified to homogeneity. The sliding movement of mutant actin filaments on heavy meromyosin attached to a glass surface was measured to assess the effect of the mutation on the motility of actin. For two C-terminal mutants, force generated by a single actin filament and myosin was also measured. These measurements indicated that both D24/D25 and E99/E100 are involved in ATP-driven sliding, whereas E360/E361/D363/E364 are not essential for ATP-driven sliding and force generation.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=46038Documentos Relacionados
- ATP-driven steady-state exchange of monomeric and filamentous actin from Dictyostelium discoideum.
- ATP-driven Ca2+/H+ antiport in acid vesicles from Dictyostelium.
- Dynamic Properties of Nucleosomes during Thermal and ATP-Driven Mobilization
- ATP-driven sodium pump in Streptococcus faecalis.
- ATP-driven stepwise rotation of FoF1-ATP synthase