ArticleOncotarget2016
Biochemical and structural characterization of a DNA N6-adenine methyltransferase from Helicobacter pylori.
Article in Oncotarget, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- Single Staphylococcus aureus SauUSI restriction enzyme motors fragment methylated DNA.Nature chemical biology · 2026Article
- Dataset from a human-in-the-loop approach to identify functionally important protein residues from literature.Scientific data · 2024Article
- 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
- Characterisation of Type II DNA Methyltransferases ofMicroorganisms · 2023Article
- Bacterial DNA methyltransferase: A key to the epigenetic world with lessons learned from proteobacteria.Frontiers in microbiology · 2023Review
- Decoding the Mechanism of Specific RNA Targeting by Ribosomal Methyltransferases.ACS chemical biology · 2022Article
- Beta class amino methyltransferases from bacteria to humans: evolution and structural consequences.Nucleic acids research · 2020Review
- The cell cycle-regulated DNA adenine methyltransferase CcrM opens a bubble at its DNA recognition site.Nature communications · 2019Article
- Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DNA N6-methyladenine modification plays an important role in regulating a variety of biological functions in bacteria. However, the mechanism of sequence-specific recognition in N6-methyladenine modification remains elusive. M1.HpyAVI, a DNA N6-adenine methyltransferase from Helicobacter pylori, shows more promiscuous substrate specificity than other enzymes. Here, we present the crystal structures of cofactor-free and AdoMet-bound structures of this enzyme, which were determined at resolutions of 3.0 Å and 3.1 Å, respectively. The core structure of M1.HpyAVI resembles the canonical AdoMet-dependent MTase fold, while the putative DNA binding regions considerably differ from those of the other MTases, which may account for the substrate promiscuity of this enzyme. Site-directed mutagenesis experiments identified residues D29 and E216 as crucial amino acids for cofactor binding and the methyl transfer activity of the enzyme, while P41, located in a highly flexible loop, playing a determinant role for substrate specificity. Taken together, our data revealed the structural basis underlying DNA N6-adenine methyltransferase substrate promiscuity.
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