Structure of helical RecA-DNA complexes. III. The structural polarity of RecA filaments and functional polarity in the RecA-mediated strand exchange reaction.
Details
Serval ID
serval:BIB_A8E994F40B42
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Structure of helical RecA-DNA complexes. III. The structural polarity of RecA filaments and functional polarity in the RecA-mediated strand exchange reaction.
Journal
Journal of Molecular Biology
ISSN
0022-2836[print], 0022-2836[linking]
Publication state
Published
Issued date
08/1988
Volume
202
Number
3
Pages
659-662
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
Publication Status: ppublish
Publication Status: ppublish
Abstract
The RecA protein of Escherichia coli has been used in vitro to mediate a strand-exchange reaction between homologous DNA molecules. A three-dimensional reconstruction of a RecA filament on double-stranded DNA has been previously determined from electron micrographs, and the reconstruction displays a clear axial polarity. The RecA-mediated strand-exchange reaction between a double-stranded DNA and a homologous single-stranded DNA that is complexed with a RecA helical polymer proceeds with a known polarity. Using image analysis of electron micrographs, we have determined the relation between the structural polarity of RecA filaments and the 3' and 5' polarity of single-stranded DNA. Thus, the structural polarity of RecA filaments can now be related to the direction in which the RecA-mediated strand-exchange reaction advances along the complexed single-stranded DNA.
Keywords
DNA, Bacterial/metabolism, Escherichia coli/metabolism, Models, Biological, Nucleic Acid Conformation, Protein Conformation, Rec A Recombinases/metabolism
Pubmed
Web of science
Create date
24/01/2008 11:36
Last modification date
20/08/2019 16:13
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