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A single amino acid substitution (Y78R) at thedimerdimer interface of homotetrameric single stranded DNA binding protein fromE.coli (EcoSSB) renders the protein a stable dimer. This dimer can bindsinglestranded DNA albeit with greatly reduced affinity. In vivo this dimericSSB cannot replace homotetrameric EcoSSB. Amino acid changes at the rim of thedimerdimer interface nearby (Q76K, Q76E) show an electrostatic interactionbetween a charged amino acid at position 76 and bound nucleic acid. Inconclusion, nucleic acid binding to homotetrameric SSB must take place acrossboth dimers to achieve functionally correct binding.

A Dimeric Mutant of the Homotetrameric Single-Stranded DNA Binding Protein from Escherichia coli