ArticleNucleic acids research2001
A dual role for substrate S-adenosyl-L-methionine in the methylation reaction with bacteriophage T4 Dam DNA-[N6-adenine]-methyltransferase.
Article in Nucleic acids research, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 34 citations in OpenAlex.
- Organization of the BcgI restriction-modification protein for the transfer of one methyl group to DNA.Nucleic acids research · 2013Article
- Time-resolved fluorescence studies of nucleotide flipping by restriction enzymes.Nucleic acids research · 2009Article
- DNA base flipping by both members of the PspGI restriction-modification system.Nucleic acids research · 2008Article
- Nucleotide flipping by restriction enzymes analyzed by 2-aminopurine steady-state fluorescence.Nucleic acids research · 2007Article
- Structure, function and mechanism of exocyclic DNA methyltransferases.The Biochemical journal · 2006Review
- Epigenetic gene regulation in the bacterial world.Microbiology and molecular biology reviews : MMBR · 2006Article
- Dimerization of the bacterial RsrI N6-adenine DNA methyltransferase.Nucleic acids research · 2006Article
- Symmetry elements in DNA structure important for recognition/methylation by DNA [amino]-methyltransferases.Nucleic acids research · 2004Article
- Structure of the bacteriophage T4 DNA adenine methyltransferase.Nature structural biology · 2003Article
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Authors and funding
8 authors at 1 institution in 1 country.
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Abstract
The fluorescence of 2-aminopurine ((2)A)-substituted duplexes (contained in the GATC target site) was investigated by titration with T4 Dam DNA-(N6-adenine)-methyltransferase. With an unmethylated target ((2)A/A duplex) or its methylated derivative ((2)A/(m)A duplex), T4 Dam produced up to a 50-fold increase in fluorescence, consistent with (2)A being flipped out of the DNA helix. Though neither S-adenosyl-L-homocysteine nor sinefungin had any significant effect, addition of substrate S-adenosyl-L-methionine (AdoMet) sharply reduced the Dam-induced fluorescence with these complexes. In contrast, AdoMet had no effect on the fluorescence increase produced with an (2)A/(2)A double-substituted duplex. Since the (2)A/(m)A duplex cannot be methylated, the AdoMet-induced decrease in fluorescence cannot be due to methylation per se. We propose that T4 Dam alone randomly binds to the asymmetric (2)A/A and (2)A/(m)A duplexes, and that AdoMet induces an allosteric T4 Dam conformational change that promotes reorientation of the enzyme to the strand containing the native base. Thus, AdoMet increases enzyme binding-specificity, in addition to serving as the methyl donor. The results of pre-steady-state methylation kinetics are consistent with this model.
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