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Nucleic Acids Research, 1993, Vol. 21, No. 4 905-911
© 1993


MOLECULAR BIOLOGY

The M·AluI DNA-(cytosine C5)-methyltransferase has an unusually large, partially dispensable, variable region

Bohong Zhang, Tao Tao1, Geoffery G. Wilson and Robert M. Blumenthal1,*

New England BioLabs Inc., Beverly, MA 01915-5599 1Department of Microbiology, Medical College of Ohio Toledo, OH 43699-0008, USA

* To whom correspondence should be addressed

Received November 16, 1992. Revised January 9, 1993. Accepted January 9, 1993.

The DNA methyltransferase of the AluI restriction-modification system, from Arthrobacter luteus, converts cytosine to 5-methylcytosine in the sequence AGCT. The gene for this methyltransferase, aluIM, was cloned into Escherichla coli and sequenced. A 525-codon open reading frame was found, consistent with deletion evidence, and the deduced amino acid sequence revealed all ten conserved regions common to 5-methylcytosine methyltransferases. The aluIM sequence predicts a protein of Mr 59.0k, in agreement with the observed Mr making M·AluI the largest known methyltransferase from a type II restriction-modification system. M·AluI also contains the largest known variable region of any monospecific DNA methyltransferase, larger than that of most multispecific methyltransferases. In other DNA methyltransferases the variable region has been implicated as the sequence-specific target recognition domain. An in-frame deletion that removes a third of this putative target-recognition region leaves the AluI methyltransferase still fully active.


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