Nucleic Acids Research, 1992, Vol. 20, No. 22 6043-6049
© 1992
ENZYMOLOGY |
Purification and properties of the Eco57lrestriction endonuclease and methylas—prototypes of a new class (type IV)
Institute of Biotechnology FERMENTAS Graiciuno 8, 232028 Vilnius, Lithuania
* To whom correspondence should be addressed
Received July 6, 1992. Revised October 26, 1992. Accepted October 26, 1992.
The Eco57lrestriction endonuclease and methylase were purified to homogeneity from the E.coli RR1 strain carrying the eco57IRM genes on a recombinant plasmid. The molecular weight of the denaturated methylase is 63 kDa. The restriction endonuclease exists in a monomeric form with an apparent molecular weight of 104–108 kDa. R.Eco57lalso possesses methylase activity. The methylation activities of both enzymes modify the outer A residue in the target sequence 5'CTGAAG yielding N6-methyladenine. M.Eco57lmodifies both strands of the substrate while R.Eco57lmodifies only one. Only the methylase enzyme is stimulated by Ca2+ +. The restriction endonuclease shows an absolute requirement for Mg2+ and is stimulated by AdoMet. ATP has no influence on either activity of the enzymes. The subunit structure and enzymatic properties of the Eco57lenzymes distinguish them from all other restriction-modification enzymes that have been described previously. Therefore, RM.Eco57lmay be regarded as a representative of a novel class of restriction-modification systems, and we propose to classify it as type IV.
+ Present address: Cold Spring Harbor Laboratory, PO Box 100, Cold Spring Harbor, NY 11724, USA
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