Structure and function of RecA-DNA complexes.


Autoria(s): Stasiak A.; Egelman E.H.
Data(s)

01/03/1994

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