Published October 24, 1995
| Published
Journal Article
Open
RecA•oligonucleotide filaments bind in the minor groove of double-stranded DNA
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Abstract
Escherichia coli RecA protein, in the presence of ATP or its analog adenosine 5'-[γ-thio]triphosphate, polymerizes on single-stranded DNA to form nucleoprotein filaments that can then bind to homologous sequences on duplex DNA. The three-stranded joint molecule formed as a result of this binding event is a key intermediate in general recombination. We have used affinity cleavage to examine this three-stranded joint by incorporating a single thymidine-EDTA•Fe (T*) into the oligonucleotide part of the filament. Our analysis of the cleavage patterns from the joint molecule reveals that the nucleoprotein filament binds in the minor groove of an extended Watson-Crick duplex.
Additional Information
© 1995 National Academy of Sciences. Contributed by Peter B. Dervan, July 21, 1995. We thank Prof. S. C. Kowalczykowski for providing us with the RecA overexpressing strain JC12772 and a detailed protocol for isolation and purification, Amherst College for a Forris Jewett Moore Fellowship (J.W.S.), and the National Institutes of Health for grant support (GM-51747). The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.Attached Files
Published - PNAS-1995-Baliga-10393-7.pdf
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PNAS-1995-Baliga-10393-7.pdf
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Additional details
- PMCID
- PMC40803
- Eprint ID
- 66903
- Resolver ID
- CaltechAUTHORS:20160510-110521506
- Amherst College
- NIH
- GM-51747
- Created
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2016-05-18Created from EPrint's datestamp field
- Updated
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2019-11-26Created from EPrint's last_modified field