メチラーゼ
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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/11/22 10:01:10」(JST)
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HaeIII
methyltransferase / DNA. Rendered from PDB 1DCT.
A methyltransferase also known as a methylase is a type of transferase enzyme that transfers a methyl group from a donor to an acceptor.
Methylation often occurs on nucleic bases in DNA or amino acids in protein structures. Methytransferases use a reactive methyl group bound to sulfur in S-adenosyl methionine (SAM) as the methyl donor.
Contents
- 1 Function
- 2 Clinical significance
- 3 Examples
- 4 References
- 5 External links
Function
DNA methylation is often utilized to silence and regulate genes without changing the original DNA sequence, an example of epigenetic modification. This methylation occurs on cytosine residues. DNA methylation may be necessary for normal growth from embryonic stages in mammals. When mutant embryonic stem cells lacking the murine DNA methyltransferase gene were introduced to a germline of mice, they caused a recessive lethal phenotype.[1] Methylation may also be linked to cancer development, as methylation of tumor suppressor genes promotes tumorigenesis and metastasis.[2]
Site-specific methyltransferases have the same DNA target sequences as certain restriction enzymes. Methylation can also serve to protect DNA from enzymatic cleavage, since restriction enzymes are unable to bind and recognize externally modified sequences. This is especially useful in bacterial restriction modification systems that use restriction enzymes to cleave foreign DNA while keeping their own DNA protected by methylation.
Methylation of amino acids in the formation of proteins leads to more diversity of possible amino acids and, therefore, more diversity of function. The methylation reaction occurs on nitrogen atoms either on the N terminus or on the side-chain position of the protein and are usually irreversible.
Clinical significance
A methylase that alters the ribosomal RNA binding site of the antibiotic linezolid causes cross-resistance to other antibiotics that act on the ribosomal RNA. Plasmid vectors capable of transmitting this gene are a cause of potentially dangerous cross resistance.[3]
Examples
Examples include:
- Catechol-O-methyl transferase
- DNA methyltransferase
- Histone methyltransferase
- 5-Methyltetrahydrofolate-homocysteine methyltransferase
- O-methyltransferase
References
- ^ Li E, Bestor TH, Jaenisch R (June 1992). "Targeted mutation of the DNA methyltransferase gene results in embryonic lethality". Cell 69 (6): 915–26. doi:10.1016/0092-8674(92)90611-F. PMID 1606615.
- ^ Laird PW, Jaenisch R (1994). "DNA methylation and cancer". Hum. Mol. Genet. 3 Spec No: 1487–95. PMID 7849743.
- ^ Morales G, Picazo JJ, Baos E, Candel FJ, Arribi A, Peláez B, Andrade R, de la Torre MA, Fereres J, Sánchez-García M (March 2010). "Resistance to linezolid is mediated by the cfr gene in the first report of an outbreak of linezolid-resistant Staphylococcus aureus". Clin. Infect. Dis. 50 (6): 821–5. doi:10.1086/650574. PMID 20144045.
External links
- Methyltransferases at the US National Library of Medicine Medical Subject Headings (MeSH)
- 3-D Structure of DNA Methyltransferase
- A novel methyltransferase : the 7SK snRNA Methylphosphate Capping Enzyme as seen on Flintbox
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Transferase: one carbon transferases (EC 2.1)
|
|
| 2.1.1: Methyl- |
| N- |
- Histamine N-methyltransferase
- Phenylethanolamine N-methyltransferase
- Amine N-methyltransferase
- Phosphatidylethanolamine N-methyltransferase
|
|
| O- |
- 5-hydroxyindole-O-methyltransferase/Acetylserotonin O-methyltransferase
- Catechol-O-methyl transferase
|
|
| Homocysteine |
- Betaine-homocysteine methyltransferase
- Homocysteine methyltransferase
- Methionine synthase
|
|
| Other |
- Phosphatidyl ethanolamine methyltransferase
- DNMT3B
- Histone methyltransferase
- Thymidylate synthase
- DNA methyltransferase
- Thiopurine methyltransferase
|
|
|
2.1.2: Hydroxymethyl-,
Formyl- and Related |
| Hydroxymethyltransferase |
- Serine hydroxymethyltransferase
- 3-methyl-2-oxobutanoate hydroxymethyltransferase
|
|
| Formyltransferase |
- Phosphoribosylglycinamide formyltransferase
- Inosine monophosphate synthase
|
|
| Other |
- Glutamate formimidoyltransferase
- Aminomethyltransferase
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|
|
| 2.1.3: Carboxy- and Carbamoyl |
| Carboxy |
- methylmalonyl-CoA carboxytransferase
|
|
| Carbamoyl |
- Aspartate carbamoyltransferase
- Ornithine carbamoyltransferase
- Oxamate carbamoyltransferase
- Putrescine carbamoyltransferase
- 3-hydroxymethylcephem carbamoyltransferase
- Lysine carbamoyltransferase
- N-acetylornithine carbamoyltransferase
|
|
|
| 2.1.4: Amidino |
- Arginine:glycine amidinotransferase
|
|
- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
|
|
|
|
UpToDate Contents
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English Journal
- Molecular mechanisms of repeated social defeat-induced glucocorticoid resistance: Role of microRNA.
- Jung SH1, Wang Y2, Kim T3, Tarr A2, Reader B2, Powell N2, Sheridan JF4.
- Brain, behavior, and immunity.Brain Behav Immun.2015 Feb;44:195-206. doi: 10.1016/j.bbi.2014.09.015. Epub 2014 Oct 12.
- Glucocorticoid (GC) resistance is a severe problem associated with various inflammatory diseases. Previous studies have shown that repeated social stress induces GC resistance in innate immune cells, but the underlying molecular mechanisms have not been fully elucidated. Therefore, the purpose of th
- PMID 25317829
- β-Arrestin1 promotes the self-renewal of the leukemia-initiating cell-enriched subpopulation in B-lineage acute lymphoblastic leukemia related to DNMT1 activity.
- Shu Y1, Zhou X1, Qi X2, Liu S2, Li K3, Tan J3, Liu Z1, Yu J4, Zhang P1, Zou L5.
- Cancer letters.Cancer Lett.2015 Feb 1;357(1):170-8. doi: 10.1016/j.canlet.2014.11.025. Epub 2014 Nov 15.
- The self-renewal ability of the leukemia initiating cell-enriched subpopulation is critical for leukemia initiation and maintenance. However, the regulation of leukemia initiating cells for the leukemia progression is poorly understood. In this study, we observed that β-Arrestin1, a multiple-functi
- PMID 25444908
- One-pot synthesis of GO/AgNPs/luminol composites with electrochemiluminescence activity for sensitive detection of DNA methyltransferase activity.
- Zhao HF1, Liang RP1, Wang JW1, Qiu JD2.
- Biosensors & bioelectronics.Biosens Bioelectron.2015 Jan 15;63:458-64. doi: 10.1016/j.bios.2014.07.079. Epub 2014 Aug 12.
- DNA methyltransferases catalyze the transfer of a methyl group from S-adenosylmethionine to the target adenine or cytosine, eventually inducing the DNA methylation in both prokaryotes and eukaryotes. Herein, we developed a novel electrochemiluminescence biosensor to quantify DNA adenine methylation
- PMID 25129507
Japanese Journal
- Epigenetic regulation of the tissue-specific expression of human UDP-glucuronosyltransferase (UGT) 1A10
- Latency of Klebsiella species and Escherichia coli strains that harbor a conjugative IncA/C type plasmid carrying both rmtB and bla_<CTX-M-14>
- Identification of <i>gntK</i>, a gene required for the methylation of purpurosamine C-6′ in gentamicin biosynthesis
- The Journal of General and Applied Microbiology 58(5), 349-356, 2012
- NAID 130004449342
Related Links
- HaeIII methyltransferase / DNA. Rendered from PDB 1DCT. Methyl-Group. Methylation Sites on DNA. A methyltransferase also known as a methylase is a type of transferase enzyme that transfers a methyl group from a donor to an acceptor.
★リンクテーブル★
[★]
- 英
- [[]]
- 同
- methylase
- 関
- [[]]
- 同
- methylase
[★]
DNAシトシンメチラーゼ
- 関
- cytosine-specific DNA-methyltransferase
[★]
DNAアデニンメチラーゼ
- 関
- adenine-specific DNA-methyltransferase
[★]
ニトロアニソール-O-デメチラーゼ
[★]
トランスメチラーゼ