DNA-methyltransferase SsoII as a bifunctional protein: Features of the interaction with the promoter region of SsoII restriction-modification genes

A. S. Romanenkov, O. V. Kisil, T. S. Zatsepin, O. V. Yamskova, A. S. Karyagina, V. G. Metelev, T. S. Oretskaya, E. A. Kubareva

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)

Abstract

DNA duplexes bearing an aldehyde group at the 2′-position of the sugar moiety were used for affinity modification of (cytosine-5)-DNA methyltransferase SsoII. It is shown that lysine residues of M.SsoII N-terminal region are located in proximity to DNA sugar-phosphate backbone of a regulatory sequence of promoter region of SsoII restriction-modification enzyme coding genes. The ability of the two M.SsoII subunits to interact with DNA regulatory sequence has been demonstrated by affinity modification using DNA duplexes with two 2′-aldehyde groups. Changes in nucleotide sequence of one half of the regulatory region prevented cross-linking of the second M.SsoII subunit. The results on sequential affinity modification of M.SsoII by two types of modified DNA ligands (i.e. by 2′-aldehyde-containing and phosphoryldisulfide- containing) have demonstrated the possibility of covalent attachment of the protein to two different DNA recognition sites: regulatory sequence and methylation site.

Original languageEnglish
Pages (from-to)1341-1349
Number of pages9
JournalBiochemistry (Moscow)
Volume71
Issue number12
DOIs
Publication statusPublished - Dec 2006
Externally publishedYes

Keywords

  • (cytosine-5)-DNA methyltransferases
  • 2′-aldehyde group
  • Affinity modification
  • Modified oligonucleotides
  • Phosphoryldisulfide group

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