JBC Transcription and Nuclear Factor Monoclonals

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Originally published In Press as doi:10.1074/jbc.M003350200 on July 3, 2000

J. Biol. Chem., Vol. 275, Issue 40, 30878-30885, October 6, 2000
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Novel Subtype of Type IIs Restriction Enzymes
BfiI ENDONUCLEASE EXHIBITS SIMILARITIES TO THE EDTA-RESISTANT NUCLEASE Nuc OF SALMONELLA TYPHIMURIUM*

Rimantas SapranauskasDagger , Giedrius SasnauskasDagger , Arunas Lagunavicius, Giedrius Vilkaitis, Arvydas Lubys, and Virginijus Siksnys§

From the Institute of Biotechnology, Graiciuno 8, Vilnius 2028, Lithuania

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 bisulfite-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 nonspecific 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 nonspecific 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.

* This work was supported by MBI Fermentas.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AJ290970.

Dagger Both authors contributed equally to this work and should be treated as joint first authors.

§ To whom correspondence should be addressed. Tel.: 370-2-602108, Fax: 370-2-602116; E-mail: siksnys@ibt.lt.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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