Synthesis of a sequence-specific DNA-cleaving peptide.
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.
D001426:Bacterial Proteins / Q000378:metabolism*; D004247:DNA / Q000378:metabolism*; D004254:DNA Nucleotidyltransferases / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000138:chemical synthesis*; D004492:Edetic Acid; D005296:Ferrous Compounds; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D010084:Oxidation-Reduction; D010446:Peptide Fragments; D011485:Protein Binding; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D005296:Ferrous Compounds; D010446:Peptide Fragments; D004247:DNA; D004492:Edetic Acid; D004254:DNA Nucleotidyltransferases; C059997:Hin recombinase