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. 1987 Apr;6(4):1137-42.
doi: 10.1002/j.1460-2075.1987.tb04869.x.

Organization of multispecific DNA methyltransferases encoded by temperate Bacillus subtilis phages

B Behrens, M Noyer-Weidner, B Pawlek, R Lauster, T S Balganesh, T A Trautner

Organization of multispecific DNA methyltransferases encoded by temperate Bacillus subtilis phages

B Behrens et al. EMBO J. 1987 Apr.

Abstract

B. subtilis phage rho 11s codes for a multispecific DNA methyltransferase (Mtase) which methylates cytosine within the sequences GGCC and GAGCTC. The Mtase gene of rho 11s was isolated and sequenced. It has 1509 bp, corresponding to 503 amino acids (aa). The enzyme's Mr of 57.2 kd predicted from the nucleotide sequence was verified by direct Mr determinations of the Mtase. A comparison of the aa sequence of the rho 11s Mtase with those of related phages SPR and phi 3%, which differ in their methylation potential, revealed generalities in the building plan of such enzymes. At least 70% of the aa of each enzyme are contained in two regions of 243 and 109 aa at the N and C termini respectively, which are highly conserved among the three enzymes. In each enzyme, variable sequences separate the conserved regions. Variability is generated through the single or multiple use of related and unrelated sequence motifs. We propose that the recognition of those DNA target sequences, which are unique for each of the three enzymes, is determined by these variable regions. Evolutionary relationships between the three enzymes are discussed.

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