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The M protein, however, can methylate on its own.
Due to structural constraints, Dot1 is only able to methylate histone H3.
It has been reported that some microbes can methylate polonium by the action of methylcobalamin.
Its ability to methylate N-heterocycles is exploited in certain deprotection schemes.
The resulting complex can both cleave and methylate DNA.
PKS-I can also methylate the α carbon of the substrate.
Strains of bacteria without this protein, or lacking the ability to methylate and demethylate them were unable to respond to stimuli.
Most commonly, MeSO is employed to methylate phenols.
S-Adenosyl methionine can subsequently methylate the amine of phosphatidylethanolamines to yield phosphatidylcholines.
A possible homolog of Dot1 was found in archaea which shows the ability to methylate archaeal histone-like protein in recent studies.
De novo methyltransferases recognize something in the DNA that allows them to newly methylate cytosines.
The recombinant YbiN protein is able to methylate partially deproteinized 50 S ribosomal subunit.
Most eukaryotes methylate only a small percentage of these sites, but 70-80% of CpG cytosines are methylated in vertebrates.
Such enzymes recognise a specific sequence in DNA and methylate a cytosine in that sequence.
In mammalian cells, cytosine-specific methyltransferases methylate certain CpG sequences, which are believed to modulate gene expression and cell differentiation.
This enzyme from the halophilic methanoarchaeon Methanohalophilus portucalensis can methylate glycine and all of its intermediates to form the compatible solute betaine.
Respectively, these enzymes oxidise monoamines (including catecholamines) and methylate the hydroxal groups of the phenyl moiety of catecholamines.
This relaxed substrate specificity requirement allows it to methylate unusual structures like DNA slippage intermediates at de novo rates that equal its maintenance rate.
These proteins include integrases, methyltransferases that might methylate DNA, proteins that inhibit restriction enzymes and radC genes.
DNMT3 is a family of DNA methyltransferases that could methylate hemimethylated and unmethylated CpG at the same rate.
This established the principle of RNA-guided genome modifications, but the generality of this process was uncertain because not all organisms methylate their DNA.
Once the plasmid begins to replicate, the methylation enzyme will be produced and methylate the plasmid DNA, protecting it from a specific restriction enzyme.
The putative temperature-sensitive endonuclease was purified from bacteria carrying this plasmid and the ability to cleave and methylate plasmid DNA was investigated.
If this enzyme reaches a "hemimethylated" portion of DNA (where methylcytosine is in only one of the two DNA strands) the enzyme will methylate the other half.
Wilson and Jones used preparations of half-methylated DNA to test the effects of a battery of carcinogens on the ability of the maintenance methylase to methylate the unmethylated strand.
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