Variability in the nucleic acid binding site size and the amount of single‐stranded DNA‐binding protein in Escherichia coli
Open Access
- 11 February 1985
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 181 (1) , 133-137
- https://doi.org/10.1016/0014-5793(85)81128-5
Abstract
The Escherichia coli single‐stranded DNA binding protein (SSB), essential for DNA replication, recombination and repair, can undergo a thermally induced irreversible conformational change which does not eliminate its biological activity, but changes the number of nucleotides it covers (binding site size) when binding to a single‐stranded nucleic acid lattice. The binding site size of native and conformationally changed SSB was also found to be a function of the molecular mass of the polynucleotide, an observation which is unusual for single‐stranded DNA binding proteins and will greatly affect the affinity relationship of this protein for nucleic acids. A radioimmunoassay used to quantitate in SSB level in cells revealed the number of SSB tetramers to be larger than initial estimates by a factor of as much as six. All these data suggest that the biological role of SSB and its mechanism of action is by far more complex than originally assumed.Keywords
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