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Synthesis of a sequence-specific DNA-cleaving peptide.
Sluka, J P; Horvath, S J; Bruist, M F; Simon, M I; Dervan, P B.
  • Sluka JP; Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125.
Science ; 238(4830): 1129-32, 1987 Nov 20.
Article en En | MEDLINE | ID: mdl-3120311
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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Banco de datos: MEDLINE Asunto principal: Proteínas Bacterianas / ADN / Proteínas de Unión al ADN / ADN Nucleotidiltransferasas Idioma: En Año: 1987 Tipo del documento: Article
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Banco de datos: MEDLINE Asunto principal: Proteínas Bacterianas / ADN / Proteínas de Unión al ADN / ADN Nucleotidiltransferasas Idioma: En Año: 1987 Tipo del documento: Article