[Probing of contacts between EcoRII DNA methyltransferase and DNA using substrate analogs and molecular modeling].
To determine the molecular mechanism of DNA recognition and catalysis by EcoRII DNA-methyltransferase (M.EcoRII) binding and methylation by the enzyme of 14-mer substrate analogs containing 2-aminopurine or 1',2'-dideoxy-D-ribofuranose in the M.EcoRII recognition site have been studied. Efficiencies of methylation and DNA binding affinities depend on the location of modified nucleoside residues within the M.EcoRII recognition site. A structural model of M.EcoRII in complex with substrate DNA and cofactor analog S-adenosyl-L-homocysteine (AdoHcy) was built using the previously solved structures of Hhal and HaeIII DNA-methyltransferases as templates. The model was constructed according to the recently developed "Frankenstein's monster" approach. Based on the model, amino acid residues taking part in interactions with DNA were predicted. Besides, based on both theoretical and experimental data obtained the groups of atoms of the heterocyclic bases within the M.EcoRII recognition site presumably involved in interaction with the enzyme were proposed.
Kudan
E V
EV
Brevnov
M G
MG
Subach
O M
OM
Rechkoblit
O A
OA
Buĭnitskiĭ
Ia M
IaM
Gromova
E S
ES
D003067:Coenzymes / Q000737:chemistry* / Q000378:metabolism; D004247:DNA / Q000737:chemistry* / Q000378:metabolism; D015257:DNA-Cytosine Methylases / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology*; D008958:Models, Molecular; D011485:Protein Binding / Q000502:physiology; D017434:Protein Structure, Tertiary; D012435:S-Adenosylhomocysteine / Q000737:chemistry* / Q000378:metabolism; D013379:Substrate Specificity
D003067:Coenzymes; D004247:DNA; D012435:S-Adenosylhomocysteine; C029528:DNA modification methylase EcoRII; D015257:DNA-Cytosine Methylases