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Science 20 November 1987:
Vol. 238. no. 4830, pp. 1129 - 1132
DOI: 10.1126/science.3120311
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Articles
Science, Vol 238, Issue 4830, 1129-1132
Copyright © 1987 by American Association for the Advancement of Science
Synthesis of a sequence-specific DNA-cleaving peptide
JP Sluka,
SJ Horvath,
MF Bruist,
MI Simon,
and
PB Dervan
Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125.
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.
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