Abstract
RecA is a multifunctional enzyme which plays a role in general recombination and in DNA repair in E. coli. It consists of 352 amino acids and has a molecular weight of 37,842. A portion of the amino terminal domain shows homology with the active sites of serine proteases and has been implicated as the active site for cleavage of the LexA repressor. It also exhibits a DNA-de-pendent ATPase activity. The protein forms helical filaments under certain conditions either alone or in complex with DNA. It is thought that the filaments play a significant physiological role in recombination events. However, the mechanism of this function is not yet clear. Electron microscopic studies on frozen hydrated filaments of RecA and RecA-DNA complexes may provide useful information about various functional states.
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