Skip Navigation

This Article
Right arrow Print PDF (1873K)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (51)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Dombroski, D.F.
Right arrow Articles by Morgan, A.R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Dombroski, D.F.
Right arrow Articles by Morgan, A.R.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1983, Vol. 11, No. 21 7487-7504
© 1983

CHEMISTRY

Studies of the interaction of RecA protein with DNA

D.F. Dombroski, D.G. Scraba, R.D. Bradley and A.R. Morgan

Department of Biochemistry, University of Alberta Edmonton, Alberta, T6G 2H7, Canada

Received June 28, 1983. Revised September 28, 1983. Accepted September 28, 1983.

Ethidium fluorescence assays were adapted for the rapid and sensitive detection of precA; in addition, fluorescence measurements on binding precA to linear, OC and CCC PM2 DNAs have enabled the 8toichiometry of precA binding as well as the precA-lnduced unwinding angle of DNA to be determined. The stoichiom-etry of binding was independently confirmed by sedimentation analysis to be one precA molecule per 3 bp. The unwinding angle was also independently confirmed by measurements of fluorescence changes induced by the binding of precA to CCC DNA which was relaxed by topoisomerase to give a precA-induced unwinding angle of 51°. Electron microscopy of OC DHA molecules which bound non-saturating amounts of precA revealed that the length increase in DNA due to precA was approximately 55%. Finally, examination of negatively stained precA complexes with a variety of linear DNAs showed that the minor groove is the primary site of interaction for this protein.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Microbiol. Mol. Biol. Rev.Home page
A. Kuzminov
Recombinational Repair of DNA Damage in Escherichia coli and Bacteriophage lambda
Microbiol. Mol. Biol. Rev., December 1, 1999; 63(4): 751 - 813.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. K. Jain, M. M. Cox, and R. B. Inman
Occurrence of Three-stranded DNA within a RecA Protein Filament
J. Biol. Chem., March 3, 1995; 270(9): 4943 - 4949.
[Abstract] [Full Text] [PDF]

Home page
 ScienceHome page
E. Egelman and X Yu
The location of DNA in RecA-DNA helical filaments
Science, July 28, 1989; 245(4916): 404 - 407.
[Abstract] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.