Molecular design and functional organization of the RecA protein.
The bacterial RecA protein participates in a remarkably diverse set of functions, all of which are involved in the maintenance of genomic integrity. RecA is a central component in both the catalysis of recombinational DNA repair and the regulation of the cellular SOS response. Despite the mechanistic differences of its functions, all require formation of an active RecA/ATP/DNA complex. RecA is a classic allosterically regulated enzyme, and ATP binding results in a dramatic increase in DNA binding affinity and a cooperative assembly of RecA subunits to form an ordered, helical nucleoprotein filament. The molecular events that underlie this ATP-induced structural transition are becoming increasingly clear. This review focuses on descriptions of our current understanding of the molecular design and allosteric regulation of RecA. We present a comprehensive list of all published recA mutants and use the results of various genetic and biochemical studies, together with available structural information, to develop ideas regarding the design of RecA functional domains and their catalytic organization.
McGrew
Dharia A
DA
Department of Biochemistry and Molecular Pharmacology, Aaron Lazare Research Building, University of Massachusetts Medical School, 364 Plantation Street, Worcester, MA 01605-2324, USA.
Knight
Kendall L
KL
D000494:Allosteric Regulation; D001419:Bacteria / Q000235:genetics*; D001665:Binding Sites; D016384:Consensus Sequence; D004260:DNA Repair; D004268:DNA-Binding Proteins / Q000502:physiology; D029968:Escherichia coli Proteins / Q000502:physiology; D009154:Mutation; D011938:Rec A Recombinases / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D011995:Recombination, Genetic; D013014:SOS Response, Genetics
D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D011938:Rec A Recombinases