title: Structure and function of RecA-DNA complexes.
abstract: While the E. coli RecA protein has been the most intensively studied enzyme of homologous recombination, the unusual RecA-DNA filament has stood alone until very recently. It now appears that this protein is part of a universal family that spans all of biology, and the filament that is formed by the protein on DNA is a universal structure. With RecA's role in recombination given new and greatly increased significance, we focus in this review on the energetics of the RecA-mediated strand exchange and the relation between the energetics and recombination spanning heterologous inserts.
authors.affiliation: Laboratoire d'Analyse Ultrastructurale, Bâtiment de Biologie, Université de Lausanne, Switzerland.
authors.forename: A
authors.initials: A
authors.lastname: Stasiak
authors.forename: E H
authors.initials: EH
authors.lastname: Egelman
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D004247:DNA / Q000737:chemistry; D004277:DNA, Single-Stranded / Q000737:chemistry; D003852:Deoxyribonucleoproteins / Q000737:chemistry / Q000648:ultrastructure*; D008958:Models, Molecular; D011938:Rec A Recombinases / Q000737:chemistry / Q000235:genetics*; D011995:Recombination, Genetic
chemical_list: D004277:DNA, Single-Stranded; D003852:Deoxyribonucleoproteins; D000255:Adenosine Triphosphate; D004247:DNA; D011938:Rec A Recombinases