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Interaction of deoxyinosine 3'-endonuclease from Escherichia coli with DNA containing deoxyinosine



Interaction of deoxyinosine 3'-endonuclease from Escherichia coli with DNA containing deoxyinosine



Journal of Biological Chemistry 270(48): 28609-28616



By using a band mobility shift assay, deoxyinosine 3'-endonuclease, an Escherichia coli enzyme which recognizes deoxyinosine, AP site, urea residue, and base mismatches in DNA, was shown to bind tightly to deoxyinosine-containing oligonucleotide duplexes. Two distinct protein-DNA complexes were observed, the faster migrating complex (complex I, K-d = 4 times 10-9 M) contained one molecule of deoxyinosine 3'-endonuclease, while the slower migrating complex (complex II, K-d = 4 times 10-7 M) contained two molecules of the protein bound to every molecule of duplex DNA. The endonucleolytic activity of deoxyinosine 3'-endonuclease paralleled the formation of the complex I. Interestingly, deoxyinosine 3'-endonuclease exhibited similar affinities for both the substrate and the nicked duplex product and thus remained bound to the DNA after the cleavage reaction. The formation of a stable complex required the presence of a duplex structure 5' to the deoxyinosine residue. DNase I footprinting revealed that deoxyinosine 3'-endonuclease protected 4-5 nucleotides 5' to the deoxyinosine, and when complex II was formed, at least 13 nucleotides 3' to deoxyinosine were protected. Based on these results, a model is proposed for the interaction of deoxyinosine 3'-endonuclease with DNA containing deoxyinosine.

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Accession: 008892016

Download citation: RISBibTeXText

PMID: 7499377

DOI: 10.1074/jbc.270.48.28609


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