Abstract:
:The Eco57I restriction 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.Eco57I also possesses methylase activity. The methylation activities of both enzymes modify the outer A residue in the target sequence 5'CTGAAG yielding N6-methyladenine. M.Eco57I modifies both strands of the substrate while R.Eco57I modifies 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 Eco57I enzymes distinguish them from all other restriction-modification enzymes that have been described previously. Therefore, RM.Eco57I may be regarded as a representative of a novel class of restriction-modification systems, and we propose to classify it as type IV.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Janulaitis A,Petrusyte M,Maneliene Z,Klimasauskas S,Butkus Vdoi
10.1093/nar/20.22.6043keywords:
subject
Has Abstractpub_date
1992-11-25 00:00:00pages
6043-9issue
22eissn
0305-1048issn
1362-4962journal_volume
20pub_type
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