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Background  SSB (single-stranded DNA-binding) proteins play an essential role in all living cells and viruses, as they are involved in processes connected with ssDNA metabolism. There has recently been an increasing interest in SSBs, since they can be applied in molecular biology techniques and analytical methods.  Nanoarchaeum equitans , the only known representative of  Archaea  phylum Nanoarchaeota, is a hyperthermophilic, nanosized, obligatory parasite/symbiont of  Ignicoccus hospitalis .    Results  This paper reports on the  ssb -like gene cloning, gene expression and characterization of a novel nucleic acid binding protein from  Nanoarchaeum equitans  archaeon ( Neq SSB-like protein). This protein consists of 243 amino acid residues and one OB fold per monomer. It is biologically active as a monomer like as SSBs from some viruses. The  Neq SSB-like protein displays a low sequence similarity to the  Escherichia coli  SSB, namely 10% identity and 29% similarity, and is the most similar to the  Sulfolobus solfataricus  SSB (14% identity and 32% similarity). The  Neq SSB-like protein binds to ssDNA, although it can also bind mRNA and, surprisingly, various dsDNA forms, with no structure-dependent preferences as evidenced by gel mobility shift assays. The size of the ssDNA binding site, which was estimated using fluorescence spectroscopy, is 7±1 nt. No salt-dependent binding mode transition was observed.  Neq SSB-like protein probably utilizes a different model for ssDNA binding than the SSB proteins studied so far. This protein is highly thermostable; the half-life of the ssDNA binding activity is 5 min at 100°C and melting temperature (T m ) is 100.2°C as shown by differential scanning calorimetry (DSC) analysis.    Conclusion    Neq SSB-like protein is a novel highly thermostable protein which possesses a unique broad substrate specificity and is able to bind all types of nucleic acids.

plos one

Characterization of a Single-Stranded DNA-Binding-Like Protein from Nanoarchaeum equitans—A Nucleic Acid Binding Protein with Broad Substrate Specificity