ArticleNucleic acids research2000
Structure of RsrI methyltransferase, a member of the N6-adenine beta class of DNA methyltransferases.
Article in Nucleic acids research, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 86 citations in OpenAlex.
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- Biochemical and structural characterization of the first-discovered metazoan DNA cytosine-N4 methyltransferase from the bdelloid rotifer Adineta vaga.The Journal of biological chemistry · 2023Article
- Structural insights into DNA NCell discovery · 2023Article
- Bacterial DNA methyltransferase: A key to the epigenetic world with lessons learned from proteobacteria.Frontiers in microbiology · 2023Review
- Does Steric Hindrance Actually Govern the Competition between Bimolecular Substitution and Elimination Reactions?The journal of physical chemistry. A · 2022Article
- Beta class amino methyltransferases from bacteria to humans: evolution and structural consequences.Nucleic acids research · 2020Review
- Structural insight into human N6amt1-Trm112 complex functioning as a protein methyltransferase.Cell discovery · 2019Article
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- Biochemical and structural characterization of a DNA N6-adenine methyltransferase from Helicobacter pylori.Oncotarget · 2016Article
- DNA Methyltransferase Activity Assays: Advances and Challenges.Theranostics · 2016Review
- Structural basis of asymmetric DNA methylation and ATP-triggered long-range diffusion by EcoP15I.Nature communications · 2015Article
- Article
- Type III restriction endonucleases are heterotrimeric: comprising one helicase-nuclease subunit and a dimeric methyltransferase that binds only one specific DNA.Nucleic acids research · 2014Article
- Reversible RNA adenosine methylation in biological regulation.Trends in genetics : TIG · 2013Review
- Organization of the BcgI restriction-modification protein for the transfer of one methyl group to DNA.Nucleic acids research · 2013Article
- S-adenosylmethionine in liver health, injury, and cancer.Physiological reviews · 2012Review
- Methylthioadenosine/S-adenosylhomocysteine nucleosidase, a critical enzyme for bacterial metabolism.Molecular microbiology · 2011Review
- Nucleotide flipping by restriction enzymes analyzed by 2-aminopurine steady-state fluorescence.Nucleic acids research · 2007Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
DNA methylation is important in cellular, developmental and disease processes, as well as in bacterial restriction-modification systems. Methylation of DNA at the amino groups of cytosine and adenine is a common mode of protection against restriction endonucleases afforded by the bacterial methyltransferases. The first structure of an N:6-adenine methyltransferase belonging to the beta class of bacterial methyltransferases is described here. The structure of M. RSR:I from Rhodobacter sphaeroides, which methylates the second adenine of the GAATTC sequence, was determined to 1.75 A resolution using X-ray crystallography. Like other methyltransferases, the enzyme contains the methylase fold and has well-defined substrate binding pockets. The catalytic core most closely resembles the PVU:II methyltransferase, a cytosine amino methyltransferase of the same beta group. The larger nucleotide binding pocket observed in M. RSR:I is expected because it methylates adenine. However, the most striking difference between the RSR:I methyltransferase and the other bacterial enzymes is the structure of the putative DNA target recognition domain, which is formed in part by two helices on an extended arm of the protein on the face of the enzyme opposite the active site. This observation suggests that a dramatic conformational change or oligomerization may take place during DNA binding and methylation.
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