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J Mol Biol. 2013 Nov 29;425(23):4802-19. doi: 10.1016/j.jmb.2013.08.021. Epub 2013 Sep 7.

Multiple C-terminal tails within a single E. coli SSB homotetramer coordinate DNA replication and repair.

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Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, 660 South Euclid Avenue, Box 8231, St. Louis, MO 63110-1093, USA.


Escherichia coli single-stranded DNA binding protein (SSB) plays essential roles in DNA replication, recombination and repair. SSB functions as a homotetramer with each subunit possessing a DNA binding domain (OB-fold) and an intrinsically disordered C-terminus, of which the last nine amino acids provide the site for interaction with at least a dozen other proteins that function in DNA metabolism. To examine how many C-termini are needed for SSB function, we engineered covalently linked forms of SSB that possess only one or two C-termini within a four-OB-fold "tetramer". Whereas E. coli expressing SSB with only two tails can survive, expression of a single-tailed SSB is dominant lethal. E. coli expressing only the two-tailed SSB recovers faster from exposure to DNA damaging agents but accumulates more mutations. A single-tailed SSB shows defects in coupled leading and lagging strand DNA replication and does not support replication restart in vitro. These deficiencies in vitro provide a plausible explanation for the lethality observed in vivo. These results indicate that a single SSB tetramer must interact simultaneously with multiple protein partners during some essential roles in genome maintenance.


DNA binding; DNA repair; DNA replication; EDTA; FRET; PBS; SIP; SSB; SSB interacting protein; ethylenediaminetetraacetic acid; fluorescence resonance energy transfer; phosphate-buffered saline; single stranded DNA binding protein; single-stranded DNA; single-stranded DNA binding protein; ssDNA; wild type; wt

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