Probing of contacts between EcoRII DNA methyltransferase and DNA with the use of substrate analogs and molecular modeling Journal Article


Authors: Koudan, E. V.; Brevnov, M. G.; Subach, O. M.; Rechkoblit, O. A.; Bujnicki, J. M.; Gromova, E. S.
Article Title: Probing of contacts between EcoRII DNA methyltransferase and DNA with the use of substrate analogs and molecular modeling
Abstract: The molecular mechanisms of DNA recognition and modification by EcoRII DNA methyltransferase (M.EcoRII) were studied using 14-mer substrate analogs containing 2-aminopurine or 1',2'-dideoxy-D-ribofuranose in the M.EcoRII recognition site. The efficiency of DNA binding and methylation depended on the position of a modified nucleoside residue in the recognition site. A structural model of M.EcoRII in complex with substrate DNA and the cofactor analog S-adenosyl-L-homocysteine (AdoHcy) was constructed using the available crystal structures of M.Hha and M.HaeIII and the recent Frankenstein's monster approach. The amino acid residues interacting with DNA were predicted based on the model. In addition, theoretical and experimental findings made it possible to predict the groups of atoms of the heterocyclic bases of the M.EcoRII recognition site that are presumably involved in the interactions with the enzyme. © 2007 Pleiades Publishing, Inc.
Keywords: methylation; binding; dna methyltransferase ecorii; homology modeling; substrate analogs
Journal Title: Molecular Biology
Volume: 41
Issue: 5
ISSN: 0026-8933
Publisher: Pleiades Publishing, Inc  
Date Published: 2007-10-01
Start Page: 806
End Page: 819
Language: English
DOI: 10.1134/s0026893307050147
PROVIDER: scopus
DOI/URL:
Notes: --- - "Export Date: 17 November 2011" - "Source: Scopus"
Altmetric
Citation Impact
MSK Authors