A. Orlova et Eh. Egelman, COOPERATIVE RIGOR BINDING OF MYOSIN TO ACTIN IS A FUNCTION OF F-ACTINSTRUCTURE, Journal of Molecular Biology, 265(5), 1997, pp. 469-474
Many aspects of cooperative behavior within pure F-actin filaments hav
e now been described. We have used two myosin fragments, heavy meromyo
sin (HMM) and Subfragment 1 (S1), to look at the rigor binding to diff
erent forms of F-actin. With Ca2+ bound at the high-affinity metal bin
ding site in actin, there is a very large cooperativity in the binding
of HMM, but no cooperativity for S1. With Mg2+ bound at the high affi
nity bo site, or with conditions that stabilize the conformation of su
bdomain-2 of actin, there is no cooperativity seen with either HMM or
S1. These results show that the two heads of HMM can induce structural
changes in F-actin that are not observed with the single head of S1.
They also support the notion that the binding of myosin to F-actin ind
uces a conformational change in subdomain-2 of actin, and that under c
ertain conditions this conformational change can be cooperatively prop
agated through an actin filament. (C) 1997 Academic Press Limited.