Published November 20, 1987
| public
Journal Article
Synthesis of a sequence-specific DNA-cleaving peptide
Abstract
A synthetic 52-residue peptide based on the sequence-specific DNA-binding domain of Hin recombinase (139-190) has been equipped with ethylenediaminetetraacetic acid (EDTA) at the amino terminus. In the presence of Fe(II), this synthetic EDTA-peptide cleaves DNA at Hin recombination sites. The cleavage data reveal that the amino terminus of Hin(139-190) is bound in the minor groove of DNA near the symmetry axis of Hin recombination sites. This work demonstrates the construction of a hybrid peptide combining two functional domains: sequence-specific DNA binding and DNA cleavage.
Additional Information
© 1987 American Association for the Advancement of Science. 15 May 1987; accepted 31 July 1987. We thank T. A. Steitz, S. B. H. Kent, and S. Mayo for helpfuil discussions. Supported by grants from the DARPA University Research Initiative Program, the National Foundation for Cancer Research, the NSF, NIH fellowship GM-09534-02 (M.F.B.), and a National Research Service Award (T32GM07616) from the National Institute of General Medical Sciences (J.P.S.).Additional details
- Eprint ID
- 54494
- Resolver ID
- CaltechAUTHORS:20150206-134713610
- Defense Advanced Research Projects Agency (DARPA)
- National Foundation for Cancer Research
- NSF
- NIH
- GM-09534-02
- National Institute of General Medical Sciences
- T32GM07616
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2015-02-07Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field