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Papers In Press, published online ahead of print July 3, 2000
Institute of Biotechnology, Vilnius LT-2028
Corresponding Author: siksnys{at}ibt.lt
The Type IIs restriction enzyme BfiI recognizes the non-palindromic nucleotide sequence 5'-ACTGGG-3' and cleaves complementary DNA strands 5/4 nucleotides downstream OF the recognition sequence. The genes coding for the BfiI restriction-modification (R-M) system were cloned/sequenced and biochemical characterization of BfiI restriction enzyme was performed. The BfiI R-M system contained three proteins: two N4-methylcytosine methyltransferases and a restriction enzyme. Sequencing of bisulphite-treated methylated DNA indicated that each methyltransferase modifies cytosines on opposite strands of the recognition sequence. The N-terminal part of the BfiI restriction enzyme amino acid sequence revealed intriguing similarities to an EDTA-resistant nuclease of Salmonella typhimurium. Biochemical analyses demonstrated that BfiI, like the nuclease of S.typhimurium, cleaves DNA in the absence of Mg2+-ions and hydrolyzes an artificial substrate bis(p-nitrophenyl) phosphate. However, unlike the non-specific S.typhimurium nuclease, BfiI restriction enzyme cleaves DNA specifically. We propose that the DNA-binding specificity of BfiI stems from the C-terminal part of the protein. The catalytic N-terminal subdomain of BfiI radically differs from that of Type II restriction enzymes and is presumably similar to the EDTA-resistant non-specific nuclease of S.typhimurium; therefore BfiI did not require metal ions for catalysis. We suggest that BfiI represents a novel subclass of Type IIs restriction enzymes that differs from the archetypal FokI endonuclease by the fold of its cleavage domain, the domain location and reaction mechanism.
J. Biol. Chem, 10.1074/jbc.M003350200
Submitted on April 19, 2000
Revised on June 15, 2000
Accepted on July 2, 2000
Novel subtype of Type IIs restriction enzymes: BfiI endonuclease exhibits similarities to the EDTA-resistant nuclease Nuc of Salmonella typhimurium
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