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Nucleic Acids Research, 2001, Vol. 29, No. 4 895-903
© 2001 Oxford University Press

Characterization of BseMII, a new type IV restriction–modification system, which recognizes the pentanucleotide sequence 5'-CTCAG(N)10/8{downarrow}

Sonata Jurenaite-Urbanaviciene, Ruta Kazlauskiene1, Virginija Urbelyte, Zita Maneliene, Maryte Petrusyte, Arvydas Lubys and Arvydas Janulaitis*

Institute of Biotechnology and 1MBI Fermentas, Graiciuno 8, 2028 Vilnius, Lithuania

We report the properties of the new BseMII restriction and modification enzymes from Bacillus stearothermophilus Isl 15-111, which recognize the 5'-CTCAG sequence, and the nucleotide sequence of the genes encoding them. The restriction endonuclease R.BseMII makes a staggered cut at the tenth base pair downstream of the recognition sequence on the upper strand, producing a two base 3'-protruding end. Magnesium ions and S-adenosyl-L-methionine (AdoMet) are required for cleavage. S-adenosylhomocysteine and sinefungin can replace AdoMet in the cleavage reaction. The BseMII methyltransferase modifies unique adenine residues in both strands of the target sequence 5'-CTCAG-3'/5'-CTGAG-3'. Monomeric R.BseMII in addition to endonucleolytic activity also possesses methyltransferase activity that modifies the A base only within the 5'-CTCAG strand of the target duplex. The deduced amino acid sequence of the restriction endonuclease contains conserved motifs of DNA N6-adenine methylases involved in S-adenosyl-L-methionine binding and catalysis. According to its structure and enzymatic properties, R.BseMII may be regarded as a representative of the type IV restriction endonucleases.

* To whom correspondence should be addressed. Tel: +370 2 602110; Fax: +370 2 602116; Email: janulait{at}ibt.lt Present address:Virginija Urbelyte, MBI Fermentas, Graiciuno 8, 2028 Vilnius, Lithuania The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors


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