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Background  Single-stranded DNA-binding proteins (SSBs) play essential roles in DNA replication, recombination and repair in Bacteria, Archaea and Eukarya. In recent years, there has been an increasing interest in SSBs, since they find numerous applications in diverse molecular biology and analytical methods.    Results  We report the characterization of single-stranded DNA-binding proteins from the psychrophilic bacteria  Desulfotalea psychrophila  ( Dps SSB),  Flavobacterium psychrophilum  ( Fps SSB),  Psychrobacter arcticus  ( Par SSB),  Psychrobacter cryohalolentis  ( Pcr SSB),  Psychromonas ingrahamii  ( Pin SSB),  Photobacterium profundum  ( Ppr SSB), and  Psychroflexus torquis  ( Pto SSB). The proteins show a high differential within the molecular mass of their monomers and the length of their amino acid sequences. The high level of identity and similarity in respect to the  Eco SSB is related to the OB-fold and some of the last amino acid residues. They are functional as homotetramers, with each monomer encoding one single stranded DNA binding domain (OB-fold). The fluorescence titrations indicated that the length of the ssDNA-binding site size is approximately 30 ± 2 nucleotides for the  Pin SSB, 31 ± 2 nucleotides for the  Dps SSB, and 32 ± 2 nucleotides for the  Par SSB,  Pcr SSB,  Ppr SSB and  Pto SSB. They also demonstrated that it is salt independent. However, when the ionic strength was changed from low salt to high, binding-mode transition was observed for the  Fps SSB, at 31 ± 2 nucleotides and 45 ± 2 nucleotides, respectively. As expected, the SSB proteins under study cause duplex DNA destabilization. The greatest decrease in duplex DNA melting temperature was observed in the presence of the  Pto SSB 17°C. The SSBs in question possess relatively high thermostability for proteins derived from cold-adapted bacteria.    Conclusion  The results showed that SSB proteins from psychrophilic microorganisms are typical bacterial SSBs and possess relatively high thermostability, offering an attractive alternative to other thermostable SSBs in molecular biology applications.

bmc microbiology

Characterization of single-stranded DNA-binding proteins from the psychrophilic bacteria Desulfotalea psychrophila, Flavobacterium psychrophilum, Psychrobacter arcticus, Psychrobacter cryohalolentis, Psychromonas ingrahamii, Psychroflexus torquis, and Photobacterium profundum