Structure and function of eukaryotic DNA methyltransferases. 2004

Taiping Chen, and En Li
Cutaneous Biology Research Center, Massachusetts General Hospital, Harvard Medical School, Charlestown, Massachusetts 02129, USA.

DNA methylation is a common epigenetic modification found in eukaryotic organisms ranging from fungi to mammals. Over the past 15 years, a number of eukaryotic DNA methyltransferases have been identified from various model organisms. These enzymes exhibit distinct biochemical properties and biological functions, partly due to their structural differences. The highly variable N-terminal extensions of these enzymes harbor various evolutionarily conserved domains and motifs, some of which have been shown to be involved in functional specializations. DNA methylation has divergent functions in different organisms, consistent with the notion that it is a dynamically evolving mechanism that can be adapted to fulfill various functions. Genetic studies using model organisms have provided evidence suggesting the progressive integration of DNA methylation into eukaryotic developmental programs during evolution.

UI MeSH Term Description Entries
D004248 DNA (Cytosine-5-)-Methyltransferases Enzymes that catalyzes the transfer of a methyl group from S-ADENOSYLMETHIONINE to the 5-position of CYTOSINE residues in DNA. DNA (Cytosine-5-)-Methyltransferase,DNA Cytosine-5-Methylase,DNA (Cytosine 5) Methyltransferase,Cytosine-5-Methylase, DNA,DNA Cytosine 5 Methylase
D004268 DNA-Binding Proteins Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases. DNA Helix Destabilizing Proteins,DNA-Binding Protein,Single-Stranded DNA Binding Proteins,DNA Binding Protein,DNA Single-Stranded Binding Protein,SS DNA BP,Single-Stranded DNA-Binding Protein,Binding Protein, DNA,DNA Binding Proteins,DNA Single Stranded Binding Protein,DNA-Binding Protein, Single-Stranded,Protein, DNA-Binding,Single Stranded DNA Binding Protein,Single Stranded DNA Binding Proteins
D005656 Fungal Proteins Proteins found in any species of fungus. Fungal Gene Products,Fungal Gene Proteins,Fungal Peptides,Gene Products, Fungal,Yeast Proteins,Gene Proteins, Fungal,Peptides, Fungal,Proteins, Fungal
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000076123 DNA (Cytosine-5-)-Methyltransferase 1 A DNA (cytosine-5-)-methyltransferase that contains a central CxxC type zinc finger motif. It binds poly(ADP)-ribose and its expression is regulated by POLY (ADP-RIBOSE) POLYMERASE-1. DNMT1 methylates CpG residues, with a preference for hemimethylated DNA, and associates with DNA replication sites in S PHASE to maintain the methylation pattern in the newly synthesized strand, which is essential for EPIGENETIC PROCESSES. It also associates with CHROMATIN during G2 PHASE and MITOSIS to maintain DNA methylation independently of replication. It is responsible for maintaining methylation patterns established in development; mutations in the DNMT1 gene are associated with HEREDITARY SENSORY NEUROPATHY TYPE 1 class E. DNMT1 Enzyme,Enzyme, DNMT1
D000090205 DNA Methyltransferase 3A A methyltransferase that catalyzes the addition of a methyl group to CYTOSINE residues of CpG dinucleotides and is required for genome-wide de novo DNA METHYLATION. DNA Methyltransferase 3 alpha,DNMT3A Protein,3A, DNA Methyltransferase,Methyltransferase 3A, DNA,Protein, DNMT3A
D000097584 DNA Methyltransferase 3B A DNA (cytosine 5) Methyltransferase that has an essential role in the establishment of DNA methylation patterns during development.
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D017434 Protein Structure, Tertiary The level of protein structure in which combinations of secondary protein structures (ALPHA HELICES; BETA SHEETS; loop regions, and AMINO ACID MOTIFS) pack together to form folded shapes. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Tertiary Protein Structure,Protein Structures, Tertiary,Tertiary Protein Structures
D018899 CpG Islands Areas of increased density of the dinucleotide sequence cytosine--phosphate diester--guanine. They form stretches of DNA several hundred to several thousand base pairs long. In humans there are about 45,000 CpG islands, mostly found at the 5' ends of genes. They are unmethylated except for those on the inactive X chromosome and some associated with imprinted genes. CpG Clusters,CpG-Rich Islands,Cluster, CpG,Clusters, CpG,CpG Cluster,CpG Island,CpG Rich Islands,CpG-Rich Island,Island, CpG,Island, CpG-Rich,Islands, CpG,Islands, CpG-Rich

Related Publications

Taiping Chen, and En Li
February 1995, BioEssays : news and reviews in molecular, cellular and developmental biology,
Taiping Chen, and En Li
January 1995, Annual review of biophysics and biomolecular structure,
Taiping Chen, and En Li
January 2011, Chembiochem : a European journal of chemical biology,
Taiping Chen, and En Li
October 2006, The Biochemical journal,
Taiping Chen, and En Li
January 2002, Critical reviews in biochemistry and molecular biology,
Taiping Chen, and En Li
January 2012, Sub-cellular biochemistry,
Taiping Chen, and En Li
April 2005, Molecular biology and evolution,
Taiping Chen, and En Li
July 1988, Biochimica et biophysica acta,
Copied contents to your clipboard!