Alw26I, Eco31I and Esp3I--type IIs methyltransferases modifying cytosine and adenine in complementary strands of the target DNA

Nucleic Acids Res. 1992 Oct 11;20(19):4981-5. doi: 10.1093/nar/20.19.4981.

Abstract

The specificity of three DNA methyltransferases M.Alw26I, M.Eco31I and M.Esp3I, isolated from Acinetobacter Iwoffi RFL26, Escherichia coli RFL31 and Hafnia alvei RFL3+, respectively, was determined. All the enzymes methylate both strands of asymmetric recognition sites yielding m5C in the top-strand and m6A in the bottom-strand, as below: 5'-GTm5CTC 5'-GGTm5CTC 5'-CGTm5CTC 3'-Cm6AGAG 3'-CCm6AGAG 3'-GCm6AGAG (M.Alw26I) (M.Eco31I) (M.Esp3I) They are the first members of type IIs methyltransferases that modify different types of nucleotides in the recognition sequence.

MeSH terms

  • Acinetobacter / enzymology*
  • Base Sequence
  • DNA Modification Methylases / metabolism*
  • DNA-Cytosine Methylases / metabolism*
  • Enterobacteriaceae / enzymology*
  • Escherichia coli / enzymology*
  • Kinetics
  • Molecular Sequence Data
  • Oligodeoxyribonucleotides / metabolism
  • Site-Specific DNA-Methyltransferase (Adenine-Specific) / metabolism*
  • Substrate Specificity

Substances

  • Oligodeoxyribonucleotides
  • DNA Modification Methylases
  • DNA modification methylase Alw26I
  • DNA modification methylase Eco31I
  • DNA modification methylase Esp3I
  • DNA-Cytosine Methylases
  • Site-Specific DNA-Methyltransferase (Adenine-Specific)