Charge-reversion mutagenesis of Dictyostelium actin to map the surface recognized by myosin during ATP-driven sliding motion - PubMed (original) (raw)

Charge-reversion mutagenesis of Dictyostelium actin to map the surface recognized by myosin during ATP-driven sliding motion

M Johara et al. Proc Natl Acad Sci U S A. 1993.

Abstract

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.

PubMed Disclaimer

References

    1. J Mol Biol. 1990 Nov 5;216(1):49-68 - PubMed
    1. Nature. 1990 Sep 6;347(6288):44-9 - PubMed
    1. Biochem J. 1990 Oct 15;271(2):407-13 - PubMed
    1. J Mol Biol. 1990 Dec 5;216(3):761-72 - PubMed
    1. Nature. 1991 Jul 25;352(6333):301-6 - PubMed

Publication types

MeSH terms

Substances

LinkOut - more resources