Dimeric/oligomeric DNA methyltransferases: an unfinished story
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Ernst G. Malygin
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.
©2009 by Walter de Gruyter Berlin New York
Artikel in diesem Heft
- Review
- Dimeric/oligomeric DNA methyltransferases: an unfinished story
- Minireview
- Induced human pluripotent stem cells: promises and open questions
- Genes and Nucleic Acids
- Effect of a quaternary pentamine on RNA stabilization and enzymatic methylation
- Protein Structure and Function
- A soluble form of ammonia monooxygenase in Nitrosomonas europaea
- Metzincin's canonical methionine is responsible for the structural integrity of the zinc-binding site
- A dual role of the N-terminal FQQI motif in GLUT4 trafficking
- Molecular Medicine
- Peritumoral administration of GPI-anchored TIMP-1 inhibits colon carcinoma growth in Rag-2 γ chain-deficient mice
- Cell Biology and Signaling
- The effect of endogenous preproneuropeptide Y leucine 7 to proline 7 polymorphism on growth and apoptosis in primary cultured HUVECs
- Cross talk between kinin and angiotensin II receptors in mouse abdominal aorta
- Advanced glycation end product accumulation in rho0 cells without a functional respiratory chain
- Proteolysis
- Association between kallikrein-related peptidases (KLKs) and macroscopic indicators of semen analysis: their relation to sperm motility
- Catalytic properties of recombinant dipeptidyl carboxypeptidase from Escherichia coli: a comparative study with angiotensin I-converting enzyme
- Pharmacological inhibitors to identify roles of cathepsin K in cell-based studies: a comparison of available tools
Artikel in diesem Heft
- Review
- Dimeric/oligomeric DNA methyltransferases: an unfinished story
- Minireview
- Induced human pluripotent stem cells: promises and open questions
- Genes and Nucleic Acids
- Effect of a quaternary pentamine on RNA stabilization and enzymatic methylation
- Protein Structure and Function
- A soluble form of ammonia monooxygenase in Nitrosomonas europaea
- Metzincin's canonical methionine is responsible for the structural integrity of the zinc-binding site
- A dual role of the N-terminal FQQI motif in GLUT4 trafficking
- Molecular Medicine
- Peritumoral administration of GPI-anchored TIMP-1 inhibits colon carcinoma growth in Rag-2 γ chain-deficient mice
- Cell Biology and Signaling
- The effect of endogenous preproneuropeptide Y leucine 7 to proline 7 polymorphism on growth and apoptosis in primary cultured HUVECs
- Cross talk between kinin and angiotensin II receptors in mouse abdominal aorta
- Advanced glycation end product accumulation in rho0 cells without a functional respiratory chain
- Proteolysis
- Association between kallikrein-related peptidases (KLKs) and macroscopic indicators of semen analysis: their relation to sperm motility
- Catalytic properties of recombinant dipeptidyl carboxypeptidase from Escherichia coli: a comparative study with angiotensin I-converting enzyme
- Pharmacological inhibitors to identify roles of cathepsin K in cell-based studies: a comparison of available tools
