Characterization of complexes between recA protein and duplex DNA by electron microscopy.

Détails

ID Serval
serval:BIB_C4277EC61207
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Characterization of complexes between recA protein and duplex DNA by electron microscopy.
Périodique
Journal of Molecular Biology
Auteur(s)
Di Capua E., Engel A., Stasiak A., Koller T.
ISSN
0022-2836[print], 0022-2836[linking]
Statut éditorial
Publié
Date de publication
05/1982
Volume
157
Numéro
1
Pages
87-103
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
Stable complexes were formed between the recA protein of Escherichia coli and duplex DNA in the presence of adenosine 5′-γ-thiotriphosphate. From the known number of base-pairs of the plasmid used, from the appearance of the complexes in the electron microscope after platinum shadowing and negative staining and from mass determinations in situ by scanning transmission electron microscopy, we deduce a structure in which 18.6 base-pairs and 6.4 recA monomers contribute to one turn of a right-handed helix with a pitch of 9.6 nm and a width of 11 nm. The results suggest an intercalative mode of binding, which partially unwinds the DNA.
ATP[S], adenosine 5′-γ-thiotriphosphate; STEM, scanning transmission electron microscope(y); FWHM, full-width half-maximum
Mots-clé
Bacterial Proteins, DNA, Escherichia coli, Macromolecular Substances, Microscopy, Electron, Microscopy, Electron, Scanning, 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
03/03/2018 21:13
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