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An extremely thermostable restriction endonuclease,Psp GI, was purified fromPyrococcus sp. strain GI-H.Psp GI is an isoschizomer ofEco RII and cleaves DNA before the first C in the sequence 5′ ^CCWGG 3′ (W is A or T).Psp GI digestion can be carried out at 65 to 85°C. To expressPsp GI at high levels, thePsp GI restriction-modification genes (pspGIR andpspGIM ) were cloned inEscherichia coli . M.Psp GI contains the conserved sequence motifs of α-aminomethyltransferases; therefore, it must be an N4-cytosine methylase. M.Psp GI shows 53% similarity to (44% identity with) its isoschizomer, M.Mva I fromMicrococcus variabilis . In a segment of 87 amino acid residues,Psp GI shows significant sequence similarity toEco RII and to regions ofSso II andSty D4I which have a closely related recognition sequence (5′ ^CCNGG 3′).Psp GI was expressed inE. coli via a T7 expression system. RecombinantPsp GI was purified to near homogeneity and had a half-life of 2 h at 95°C.Psp GI remained active following 30 cycles of thermocycling; thus, it can be used in DNA-based diagnostic applications.

applied and environmental microbiology

Characterization of an Extremely Thermostable Restriction Enzyme, Psp GI, from a Pyrococcus Strain and Cloning of the Psp GI Restriction-Modification System in Escherichia coli