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Restriction enzymes are the main defence system against foreign DNA, in charge of preserving genome integrity.  Lactococcus raffinolactis  BGTRK10-1 expresses  Lra I Type II restriction-modification enzyme, whose activity is similar to that shown for  Eco RI;  Lra I methyltransferase protects DNA from  Eco RI cleavage. The gene encoding  Lra I endonuclease was cloned and overexpressed in  E. coli . Purified enzyme showed the highest specific activity at lower temperatures (between 13°C and 37°C) and was stable after storage at −20°C in 50% glycerol. The concentration of monovalent ions in the reaction buffer required for optimal activity of  Lra I restriction enzyme was 100 mM or higher. The recognition and cleavage sequence for  Lra I restriction enzyme was determined as 5′-G/AATTC-3′, indicating that  Lra I restriction enzyme is an isoschizomer of  Eco RI. In the reaction buffer with a lower salt concentration,  Lra I exhibits star activity and specifically recognizes and cuts another alternative sequence 5′-A/AATTC-3′, leaving the same sticky ends on fragments as  Eco RI, which makes them clonable into a linearized vector. Phylogenetic analysis based on sequence alignment pointed out the common origin of  Lra I restriction-modification system with previously described  Eco RI-like restriction-modification systems.

LraI fromLactococcus raffinolactisBGTRK10-1, an Isoschizomer ofEcoRI, Exhibits Ion Concentration-Dependent Specific Star Activity