Structure and function of RecA-DNA complexes.
Data(s) |
01/03/1994
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Resumo |
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. |
Identificador |
http://serval.unil.ch/?id=serval:BIB_E942227B83F4 isbn:0014-4754[print], 0014-4754[linking] pmid:8143793 isiid:A1994NA86600003 |
Idioma(s) |
en |
Fonte |
Experientia, vol. 50, no. 3, pp. 192-203 |
Palavras-Chave | #Adenosine Triphosphate/metabolism; DNA/chemistry; DNA, Single-Stranded/chemistry; Deoxyribonucleoproteins/chemistry; Deoxyribonucleoproteins/ultrastructure; Models, Molecular; Rec A Recombinases/chemistry; Rec A Recombinases/genetics; Recombination, Genetic |
Tipo |
info:eu-repo/semantics/review article |