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

Details

Serval ID
serval:BIB_C4277EC61207
Type
Article: article from journal or magazin.
Collection
Publications
Title
Characterization of complexes between recA protein and duplex DNA by electron microscopy.
Journal
Journal of Molecular Biology
Author(s)
Di Capua E., Engel A., Stasiak A., Koller T.
ISSN
0022-2836[print], 0022-2836[linking]
Publication state
Published
Issued date
05/1982
Volume
157
Number
1
Pages
87-103
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Abstract
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
Keywords
Bacterial Proteins, DNA, Escherichia coli, Macromolecular Substances, Microscopy, Electron, Microscopy, Electron, Scanning, Protein Binding, Rec A Recombinases, Recombination, Genetic
Pubmed
Web of science
Create date
24/01/2008 10:36
Last modification date
20/08/2019 15:39
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