dam methylase from E. coli. Circular dichroism investigations of the secondary structure and influence of S-adenosylmethionine

FEBS Lett. 1987 Mar 23;213(2):297-300. doi: 10.1016/0014-5793(87)81509-0.

Abstract

The enzyme dam methylase which recognizes and methylates the adenine in the palindromic sequence GATC in DNA was isolated and the secondary structure was determined by CD spectroscopy and various predicting methods from the amino acid sequence. The interaction of dam methylase with S-adenosylmethionine was studied by CD spectroscopy indicating a decrease of the percentage of alpha-helix as the amount of S-adenosylmethionine bound to the enzyme was increased.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Circular Dichroism
  • Escherichia coli / enzymology*
  • Methyltransferases / metabolism*
  • Protein Conformation
  • S-Adenosylmethionine / metabolism*
  • Site-Specific DNA-Methyltransferase (Adenine-Specific)

Substances

  • S-Adenosylmethionine
  • Methyltransferases
  • Site-Specific DNA-Methyltransferase (Adenine-Specific)