title: Dimeric/oligomeric DNA methyltransferases: an unfinished story.
abstract: DNA methyltransferases (MTases) are enzymes that carry out post-replicative sequence-specific modifications. The initial experimental data on the structure and kinetic characteristics of the EcoRI MTase led to the paradigm that type II systems comprise dimeric endonucleases and monomeric MTases. In retrospect, this was logical because, while the biological substrate of the restriction endonuclease is two-fold symmetrical, the in vivo substrate for the MTase is generally hemi-methylated and, hence, inherently asymmetric. Thus, the paradigm was extended to include all DNA MTases except the more complex bifunctional type I and type III enzymes. Nevertheless, a gradual enlightenment grew over the last decade that has changed the accepted view on the structure of DNA MTases. These results necessitate a more complex view of the structure and function of these important enzymes.
authors.affiliation: State Research Center of Virology and Biotechnology Vector, Novosibirsk, Russia.
authors.forename: Ernst G
authors.initials: EG
authors.lastname: Malygin
authors.forename: Alexey A
authors.initials: AA
authors.lastname: Evdokimov
authors.forename: Stanley
authors.initials: S
authors.lastname: Hattman
mesh_terms: D000818:Animals; D015254:DNA Modification Methylases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D055503:Protein Multimerization
chemical_list: D015254:DNA Modification Methylases