Elongation of duplex DNA by recA protein.

Détails

ID Serval
serval:BIB_9A97143B5833
Type
Article: article d'un périodique ou d'un magazine.
Sous-type
Lettre (letter): communication adressée à l'éditeur.
Collection
Publications
Titre
Elongation of duplex DNA by recA protein.
Périodique
Journal of Molecular Biology
Auteur(s)
Stasiak A., Di Capua E., Koller T.
ISSN
0022-2836[print], 0022-2836[linking]
Statut éditorial
Publié
Date de publication
09/1981
Volume
151
Numéro
3
Pages
557-564
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
recA protein, which is essential for the recombination process in Escherichia coli, was incubated in the presence of 5′-γ-thiotriphosphate with circular plasmid pBRβG containing small single-stranded gaps. Stable complexes were formed which appear in the electron microscope as fibres with a diameter about five times that of naked DNA. Complex formation appears to be a co-operative process whereby the average rise per base-pair with respect to the fibre axis increases from 3·39 ± 0·08 Å to 5·20 ± 0·18 Å. The elongation of DNA by about 50% is compatible with an unwinding of the double helix and an intercalating mode of binding of recA and/or 5′-γ-thiotriphosphate to DNA.
Mots-clé
Bacterial Proteins/metabolism, DNA, Bacterial/metabolism, Escherichia coli/genetics, Escherichia coli/metabolism, Nucleic Acid Conformation, Plasmids, Protein Binding, Rec A Recombinases, Recombination, Genetic
Pubmed
Web of science
Création de la notice
24/01/2008 11:36
Dernière modification de la notice
20/08/2019 16:01
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