Publication Date:
1987-11-20
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sluka, J P -- Horvath, S J -- Bruist, M F -- Simon, M I -- Dervan, P B -- GM-09534-02/GM/NIGMS NIH HHS/ -- T32GM07616/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Nov 20;238(4830):1129-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3120311" target="_blank"〉PubMed〈/a〉
Keywords:
Bacterial Proteins/*metabolism
;
DNA/*metabolism
;
DNA Nucleotidyltransferases/*metabolism
;
DNA-Binding Proteins/*chemical synthesis
;
Edetic Acid
;
Ferrous Compounds
;
Models, Molecular
;
Nucleic Acid Conformation
;
Oxidation-Reduction
;
Peptide Fragments
;
Protein Binding
;
Structure-Activity Relationship
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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