ArticleJournal of molecular biology2014
The carboxy-terminal domain of ROS1 is essential for 5-methylcytosine DNA glycosylase activity.
Article in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
12 citing papers in PubMed.
- Molecular Mechanisms Underlying the Establishment, Maintenance, and Removal of DNA Methylation in Plants.Annual review of plant biology · 2025Review
- Quinoline-based compounds can inhibit diverse enzymes that act on DNA.Cell chemical biology · 2024Article
- Molecular basis of the plant ROS1-mediated active DNA demethylation.Nature plants · 2023Article
- Noncatalytic Domains in DNA Glycosylases.International journal of molecular sciences · 2022Review
- Recent Advances on DNA Base Flipping: A General Mechanism for Writing, Reading, and Erasing DNA Modifications.Advances in experimental medicine and biology · 2022Article
- Human MettL3-MettL14 RNA adenine methyltransferase complex is active on double-stranded DNA containing lesions.Nucleic acids research · 2021Article
- Active DNA Demethylation in Plants.International journal of molecular sciences · 2019Review
- DNA Base Excision Repair in Plants: An Unfolding Story With Familiar and Novel Characters.Frontiers in plant science · 2019Review
- Protecting DNA from errors and damage: an overview of DNA repair mechanisms in plants compared to mammals.Cellular and molecular life sciences : CMLS · 2017Review
- Targeted DNA demethylation in human cells by fusion of a plant 5-methylcytosine DNA glycosylase to a sequence-specific DNA binding domain.Epigenetics · 2017Article
- DNA Base Flipping: A General Mechanism for Writing, Reading, and Erasing DNA Modifications.Advances in experimental medicine and biology · 2016Review
- The Mechanisms of Generation, Recognition, and Erasure of DNA 5-Methylcytosine and Thymine Oxidations.The Journal of biological chemistry · 2015Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Arabidopsis thaliana repressor of silencing 1 (ROS1) is a multi-domain bifunctional DNA glycosylase/lyase, which excises 5-methylcytosine (5mC) and 5-hydroxymethylcytosine (5hmC) as well as thymine and 5-hydroxymethyluracil (i.e., the deamination products of 5mC and 5hmC) when paired with a guanine, leaving an apyrimidinic (AP) site that is subsequently incised by the lyase activity. ROS1 is slow in base excision and fast in AP lyase activity, indicating that the recognition of pyrimidine modifications might be a rate-limiting step. In the C-terminal half, the enzyme harbors a helix-hairpin-helix DNA glycosylase domain followed by a unique C-terminal domain. We show that the isolated glycosylase domain is inactive for base excision but retains partial AP lyase activity. Addition of the C-terminal domain restores the base excision activity and increases the AP lyase activity as well. Furthermore, the two domains remain tightly associated and can be co-purified by chromatography. We suggest that the C-terminal domain of ROS1 is indispensable for the 5mC DNA glycosylase activity of ROS1.
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