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Nucleic Acids Research, 1994, Vol. 22, No. 20 4066-4072
© 1994

RNA

M.ø3TII: a new monospecific DNA (cytosine-C5) methyltransf erase with pronounced ami no acid sequence similarity to a family of adenine-N6-DNA-methyltransferases

Mario Noyer-Weidner1, Jörn Walter, Peter-Andreas Terschüren, Sunghee Chai and Thomas A. Trautner*

Max-Planck-Institut fur molekulare Genetik, IhnestraBe 73 D-14195 Berlin

*To whom correspondence should be addressed

Received July 26, 1994. Revised September 5, 1994. Accepted September 5, 1994.

The temperate B.subtilis phages ø3T and {varrho}11s code, in addition to the multispecific DNA (cytosine-C5) methyltransf erases (C5-MTases) M.ø3TI and M.{varrho}11sl, which were previously characterized, for the identical monospecific C5-MTases M.ø3TII and M.{varrho}11SII. These enzymes modify the C of TCGA sites, a novel target specificity among C5-MTases. The primary sequence of M.ø3TII (326 amino acids) shows all conserved motifs typical of the building plan of C5-MTases. The degree of relatedness between M.ø3TII and all other mono- or multispecific C5-MTases ranges from 30 - 40% amino acid identity. Particularly M.ø3TII does not show pronounced similarity to M.ø3TI indicating that both MTase genes were not generated from one another but were acquired independently by the phage. The amino terminal part of the M.ø3TII (preceding the variable region ‘V’), which predominantly constitutes the catalytic domain of the enzyme, exhibits pronounced sequence similarity to the amino termini of a family of A-N6-MTases, which — like M.Taql — recognize the general sequence TNNA. This suggests that recently described similarities in the general three dimensional organization of C5- and A-N6-MTases imply divergent evolution of these enzymes originating from a common molecular ancestor.

1Walter de Gruyter & Co., Scientific Publishers, Genthiner StraBe 13, D-10728 Berlin, Germany


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