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Nucleic Acids Research, 1989, Vol. 17, No. 11 4161-4175
© 1989

MOLECULAR BIOLOGY

Sequence, internal homology and high-level expression of the gene for a DNA-(cytosine N4)-methyltransferase, M-Pvu II

Tao Tao, Johannes Walter1,+, Kathleen J. Brennan§,, Melissa M. Cotterman{Phi}, and Robert M. Blumenthal*,

1Cold Spring Harbor Laboratory Cold Spring Harbor, NY 11724, USA Department of Microbiology, Medical College of Ohio PO Box 10008, Toledo, OH 43699

*To whom correspondence should be addressed

Received November 18, 1988. Revised April 4, 1989. Accepted April 4, 1989.

The base sequence of the pvulIM gene has been determined. This gene codes for a DNA-(cytosine N4-methyltransferase, M.Pvu II. The base sequence contains a single large open reading frame that predicts a 38.3kDa polypeptide, consistent with experimental data. The pvulIM gene contains some sequences common to DNA methyltransferases in general, but includes none of the sequences specifically conserved among DNA-(cytosine 5)-methyltransferases. The pvulIM sequence also reveals an internal homology at the amino acid level, each half of which spans over 100 amino acids and is itself homologous to the sequences of some DNA-(adenine N5)-methyltransferases. A derivative of the pvulIM plasmid was constructed to allow high-level production of M.Pvu II. Specifically, the composite plac promoter was inserted 5' to pvulIM, intervening DNA was deleted, and the resulting construct was used to transform an mcrB laclq strain of Escherichia coli. When this transformant was induced with isopropyl-B-D-galactopyranoside (IPTG), growth rapidly ceased and M.Pvu II accumulated to the point of comprising over 10% of the total soluble protein.

+Present addresses: Department of Chemistry, University of California, Berkeley, CA 94720

§Present addresses: Department of Medicine, Thomas Jefferson School of Medicine, Philadelphia, PA 19107

{Phi}Present addresses: Bureau of Biologics, Food and Drug Administration, Bethesda, Md 20892, USA


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