A pair of single-strand and double-strand DNA cytosine-N4 methyltransferases from Bacillus centrosporus

Biol Chem. 1998 Apr-May;379(4-5):569-71.

Abstract

Sequence analysis of the BcnI restriction-modification system revealed the presence of an open reading frame encoding a second cytosine-N4 methyltransferase, M.BcnIA, in the vicinity of the genes specifying the previously characterized cytosine-N4 methyltransferase M.BcnIB and restriction endonuclease R.BcnI. Both methyltransferases were purified from the E. coli cells expressing the individual genes, and their enzymatic efficiencies in vitro were compared with a variety of DNA substrates. Both enzymes act on 5'-CC(C/G)GG-3' sites in double-stranded DNA, however, M.BcnIA can also, with a comparable efficiency, modify the specific targets in single-stranded DNA. The biological significance of the presence of the tandem methyltransferases in the BcnI system is discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus / enzymology*
  • Bacteriophage M13 / genetics
  • DNA, Single-Stranded / metabolism*
  • DNA, Viral / metabolism
  • DNA-Cytosine Methylases / metabolism*
  • Oligodeoxyribonucleotides / metabolism
  • Substrate Specificity

Substances

  • DNA, Single-Stranded
  • DNA, Viral
  • Oligodeoxyribonucleotides
  • DNA modification methylase BcnI
  • DNA-Cytosine Methylases