[Molecular enzymology of phage T4 Dam DNA-methyltransferase].
The review reflects results of studies on the molecular mechanism of phage T4 Dam DNA-methyltransferase action. The enzyme (T4Dam) catalyzes methyl group transfer from S-adenosyl-l-methionine (AdoMet) to N6-adenine position in the palindromic recognition sequence GATC (EC 2.1.1.72). The enzyme subunit structure, substrate-binding and kinetic parameters for a wide range of native and modified oligonucleotide duplexes, as well as steady-state reaction kinetic scheme, included T4Dam isomerization to catalytically active form, are considered. The found mechanisms of DNA induced T4Dam dimerization, target base flipping, enzyme reorientation in an asymmetrically modified recognition sequence, effector action of reaction substrates and processive methylation of DNA substrates, containing more than one specific site, are discussed. The results obtained with T4Dam may be useful for understanding mechanisms of action of other homologous enzymes, most of all for specimens of numerous family of Dam DNA-methyltransferases.
Zinov'ev
V V
VV
Evdokimov
A A
AA
Hattman
S
S
Malygin
E G
EG
D017122:Bacteriophage T4 / Q000201:enzymology*; D001665:Binding Sites; D019175:DNA Methylation; D019281:Dimerization; D021122:Protein Subunits; D015265:Site-Specific DNA-Methyltransferase (Adenine-Specific) / Q000502:physiology*; D013379:Substrate Specificity; D014764:Viral Proteins
D021122:Protein Subunits; D014764:Viral Proteins; C058693:Dam methyltransferase; D015265:Site-Specific DNA-Methyltransferase (Adenine-Specific); C499297:dam protein, Bacteriophage T4