ArticleBiochemistry2014
5-methylcytosine recognition by Arabidopsis thaliana DNA glycosylases DEMETER and DML3.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
13 citing papers in PubMed, 20 citations in OpenAlex.
- Occupancy-based mechanism is the chief mode of ROS1 function in preventing DNA hypermethylation.Nature plants · 2026Article
- Associations between placental hydroxymethylation and birthweight.Epigenetics reports · 2024Article
- Base Excision DNA Repair in Plants:International journal of molecular sciences · 2023Review
- Molecular basis of the plant ROS1-mediated active DNA demethylation.Nature plants · 2023Article
- The Function of DNA Demethylase Gene ROS1a Null Mutant on Seed Development in Rice (International journal of molecular sciences · 2022Article
- Structural Aspects of DNA Repair and Recombination in Crop Improvement.Frontiers in genetics · 2020Review
- Evidence for novel epigenetic marks within plants.AIMS genetics · 2019Article
- Protecting DNA from errors and damage: an overview of DNA repair mechanisms in plants compared to mammals.Cellular and molecular life sciences : CMLS · 2017Review
- Role of Base Excision "Repair" Enzymes in Erasing Epigenetic Marks from DNA.Chemical reviews · 2016Review
- DNA Base Flipping: A General Mechanism for Writing, Reading, and Erasing DNA Modifications.Advances in experimental medicine and biology · 2016Review
- Article
- Mechanisms for enzymatic cleavage of the N-glycosidic bond in DNA.Organic & biomolecular chemistry · 2014Review
- The carboxy-terminal domain of ROS1 is essential for 5-methylcytosine DNA glycosylase activity.Journal of molecular biology · 2014Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Methylation of cytosine to 5-methylcytosine (5mC) is important for gene expression, gene imprinting, X-chromosome inactivation, and transposon silencing. Active demethylation in animals is believed to proceed by DNA glycosylase removal of deaminated or oxidized 5mC. In plants, 5mC is removed from the genome directly by the DEMETER (DME) family of DNA glycosylases. Arabidopsis thaliana DME excises 5mC to activate expression of maternally imprinted genes. Although the related Repressor of Silencing 1 (ROS1) enzyme has been characterized, the molecular basis for 5mC recognition by DME has not been investigated. Here, we present a structure-function analysis of DME and the related DME-like 3 (DML3) glycosylases for 5mC and its oxidized derivatives. Relative to 5mC, DME and DML3 exhibited robust activity toward 5-hydroxymethylcytosine, limited activity for 5-carboxylcytosine, and no activity for 5-formylcytosine. We used homology modeling and mutational analysis of base excision and DNA binding to identify residues important for recognition of 5mC within the context of DNA and inside the enzyme active site. Our results indicate that the 5mC binding pocket is composed of residues from discrete domains and is responsible for discrimination against 5mC derivatives, and suggest that DME, ROS1, and DML3 utilize subtly different mechanisms to probe the DNA duplex for cytosine modifications.
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Registered trials
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