A Model for the Core Structure of the Escherichia coli RecA Protein
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Excerpt
The RecA protein of Escherichia coli is essential for homologous recombination (Clark and Margulies 1965). The recA+ gene has been sequenced and has been shown to encode a 352-amino-acid protein of 37,800 daltons (Horii et al. 1980; Sancar et al. 1980). For its size, the RecA protein exhibits a remarkable variety of reactions in vitro. The protein can induce D-loops and effect strand transfer of DNA (Cox and Lehman 1981; DasGupta et al. 1981; Kahn et al. 1981; West et al. 1981), partially unwind duplex DNA (Dunn et al. 1982; Flory and Radding 1982; Iwabuchi et al. 1983), perform a cofactor-dependent, highly specific proteolytic function (McEntee and Weinstock 1981; Little et al. 1980), and catalyze DNA-dependent ATP hydrolysis (Ogawa et al. 1979; Weinstock et al. 1981). All of these activities of RecA protein depend on its binding to ATP.
To learn how RecA protein carries out these reactions in atomic...
