Polar Destabilization of DNA Duplexes with Single-Stranded Overhangs by the Deinococcus radiodurans SSB Protein†
Identifieur interne : 002D67 ( Main/Exploration ); précédent : 002D66; suivant : 002D68Polar Destabilization of DNA Duplexes with Single-Stranded Overhangs by the Deinococcus radiodurans SSB Protein†
Auteurs : Julie M. Eggington [États-Unis] ; Alexander G. Kozlov [États-Unis] ; Michael M. Cox [États-Unis] ; Timothy M. Lohman [États-Unis]Source :
- Biochemistry [ 0006-2960 ] ; 2006.
Abstract
The Deinococcus radiodurans SSB protein has an occluded site size of 50 ± 2 nucleotides on ssDNA but can form a stable complex with a 26−30-nucleotide oligodeoxynucleotide using a subset of its four ssDNA binding domains. Quantitative estimates of D. radiodurans SSB protein in the D. radiodurans cell indicate approximately 2500−3000 dimers/cell, independent of the level of irradiation. At biologically relevant concentrations, when bound at single-strand−double-strand DNA junctions in vitro, D. radiodurans SSB protein has a limited capacity to displace the shorter strand of the duplex, permitting it to bind to single-strand extensions shorter than 26−30 nucleotides. The capacity to displace the shorter strand of the duplex shows a pronounced bias for extensions with a free 3‘ end. The Escherichia coli SSB protein has a similar but somewhat less robust capacity to displace a DNA strand annealed adjacent to a single-strand extension. These activities are likely to be relevant to the action of bacterial SSB proteins in double-strand break repair, acting at the frayed ends created by ionizing radiation.
Url:
DOI: 10.1021/bi061178m
Affiliations:
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<front><div type="abstract">The Deinococcus radiodurans SSB protein has an occluded site size of 50 ± 2 nucleotides on ssDNA but can form a stable complex with a 26−30-nucleotide oligodeoxynucleotide using a subset of its four ssDNA binding domains. Quantitative estimates of D. radiodurans SSB protein in the D. radiodurans cell indicate approximately 2500−3000 dimers/cell, independent of the level of irradiation. At biologically relevant concentrations, when bound at single-strand−double-strand DNA junctions in vitro, D. radiodurans SSB protein has a limited capacity to displace the shorter strand of the duplex, permitting it to bind to single-strand extensions shorter than 26−30 nucleotides. The capacity to displace the shorter strand of the duplex shows a pronounced bias for extensions with a free 3‘ end. The Escherichia coli SSB protein has a similar but somewhat less robust capacity to displace a DNA strand annealed adjacent to a single-strand extension. These activities are likely to be relevant to the action of bacterial SSB proteins in double-strand break repair, acting at the frayed ends created by ionizing radiation.</div>
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