ArticleNature communications2019
The cell cycle-regulated DNA adenine methyltransferase CcrM opens a bubble at its DNA recognition site.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 39 citations in OpenAlex.
- Protein loops are major contributors to DNA strand separation and high-fidelity substrate recognition for DNA methyltransferase CcrM.The Journal of biological chemistry · 2026Article
- Epigenetic regulation in prokaryotes: transcriptional and phenotypic outcomes of DNA methyltransferase activity.FEMS microbiology reviews · 2026Review
- Inhibition ofACS omega · 2025Article
- Mechanism for the substrate recognition by a eukaryotic DNA NNature communications · 2025Article
- A population model reveals a surprising role of stochastic cell division in epigenetic memory systems.iScience · 2025Article
- Structural insight into the substrate binding of the AMT complex via an inhibitor-trapped state.Protein science : a publication of the Protein Society · 2025Article
- Inhibition ofbioRxiv : the preprint server for biology · 2025Article
- Quinoline-based compounds can inhibit diverse enzymes that act on DNA.Cell chemical biology · 2024Article
- SUPREM: an engineered non-site-specific m6A RNA methyltransferase with highly improved efficiency.Nucleic acids research · 2024Article
- Burkholderia cenocepacia epigenetic regulator M.BceJIV simultaneously engages two DNA recognition sequences for methylation.Nature communications · 2024Article
- Article
- Dual RNA-Seq Analysis Pinpoints a Balanced Regulation between Symbiosis and Immunity inInternational journal of molecular sciences · 2023Article
- 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
- High fidelity DNA strand-separation is the major specificity determinant in DNA methyltransferase CcrM's catalytic mechanism.Nucleic acids research · 2023Article
- Comparative Study of Adenosine Analogs as Inhibitors of Protein Arginine Methyltransferases and aACS chemical biology · 2023Article
- Structures of MPND Reveal the Molecular Recognition of Nucleosomes.International journal of molecular sciences · 2023Article
- Structural insights into DNA NCell discovery · 2023Article
- Systematic Design of Adenosine Analogs as Inhibitors of aJournal of medicinal chemistry · 2023Article
- Bacterial DNA methyltransferase: A key to the epigenetic world with lessons learned from proteobacteria.Frontiers in microbiology · 2023Review
- Repurposing epigenetic inhibitors to target theEpigenetics · 2022Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The Caulobacter crescentus cell cycle-regulated DNA methyltransferase (CcrM) methylates the adenine of hemimethylated GANTC after replication. Here we present the structure of CcrM in complex with double-stranded DNA containing the recognition sequence. CcrM contains an N-terminal methyltransferase domain and a C-terminal nonspecific DNA-binding domain. CcrM is a dimer, with each monomer contacting primarily one DNA strand: the methyltransferase domain of one molecule binds the target strand, recognizes the target sequence, and catalyzes methyl transfer, while the C-terminal domain of the second molecule binds the non-target strand. The DNA contacts at the 5-base pair recognition site results in dramatic DNA distortions including bending, unwinding and base flipping. The two DNA strands are pulled apart, creating a bubble comprising four recognized base pairs. The five bases of the target strand are recognized meticulously by stacking contacts, van der Waals interactions and specific Watson-Crick polar hydrogen bonds to ensure high enzymatic specificity.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.