The helicity of DNA in complexes with recA protein.

Détails

ID Serval
serval:BIB_B5DF57DF9937
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
The helicity of DNA in complexes with recA protein.
Périodique
Nature
Auteur(s)
Stasiak A., Di Capua E.
ISSN
0028-0836
Statut éditorial
Publié
Date de publication
09/1982
Peer-reviewed
Oui
Volume
299
Numéro
5879
Pages
185-186
Langue
anglais
Résumé
The RecA protein of Escherichia coli is involved in recombination (for review see ref. 1). The protein binds transiently to double-stranded DNA in the presence of ATP. In the presence of ATP gamma S, a non-hydrolysable analogue of ATP, recA-DNA complexes are stable. Duplex DNA in these complexes is stretched by a factor 1.5 (ref. 4), and the complexes appear in the electron microscope as helical filaments with a pitch of approximately 100 A and 6.2 recA units per turn covering 18.6 base pairs (bp). RecA crystals have a space group of similar helical parameters. In order to understand the function of recA, it is necessary to describe the conformation of the DNA in the recA complex. Using a topological method, the present work determines the helicity of DNA in the complex. We find that the DNA helix follows the protein helix visible in the electron microscope and has 18.6 bp per turn, which corresponds to an unwinding of the DNA double helix by 15 degrees per bp.
Mots-clé
Bacterial Proteins, DNA, DNA, Bacterial, Escherichia coli, Nucleic Acid Conformation, Rec A Recombinases
Pubmed
Web of science
Création de la notice
24/01/2008 11:36
Dernière modification de la notice
20/08/2019 16:24
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