Evidence map›Paper›PMID 24678721›Full record

ArticleBiochemistry2014

5-methylcytosine recognition by Arabidopsis thaliana DNA glycosylases DEMETER and DML3.

Sonja C Brooks, Robert L Fischer, Jin Hoe Huh, Brandt F Eichman

Open access · bronzeAbstract read
In one paragraph

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.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.4field-weighted citation impact, top 18% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Base Excision DNA Repair in Plants:International journal of molecular sciences · 2023
    Review
  4. Article
  5. Article
  6. Review
  7. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 3 institutions in 2 countries.

Sonja C BrooksDepartment of Biological Sciences and Center for Structural Biology, Vanderbilt University , Nashville, Tennessee 37232, United States.
Robert L Fischer
Jin Hoe Huh
Brandt F Eichman
Vanderbilt University · USSeoul National University · KRUniversity of California, Berkeley · US

Funding

Tumor Immunology and Microenvironment Research ProgramP30CA068485 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI STACIE B DUSETZINA · 1995 to 2026
$172.8M
Structural Biology Facility CoreP30ES000267 · NIEHS · VANDERBILT UNIVERSITY · PI GUENGERICH, F PETER · 1985 to 2014
$20.3M
MOLECULAR BIOPHYSICS TRAINING PROGRAM AT VANDERBILTT32GM008320 · NIGMS · VANDERBILT UNIVERSITY · PI CHAZIN, WALTER J. · 1989 to 2023
$7.9M
Regulation and Function of DNA Demethylation in ArabidopsisR01GM069415 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI FISCHER, ROBERT L, ZILBERMAN, DANIEL · 2004 to 2016
$3.8M
Mechanisms of selective excision and oxidative repair of alkylated DNAR01ES019625 · NIEHS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI CAMPS, MANEL · 2011 to 2015
$1.7M
NCI NIH HHS P30 CA068485NIEHS NIH HHS ES019625NIEHS NIH HHS P30 ES000267NIEHS NIH HHS R01 ES019625NIGMS NIH HHS GM69415NIGMS NIH HHS R01 GM069415NIGMS NIH HHS T32 GM008320NIGMS NIH HHS T32 GM08320
6 · The paper itself

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.

Indexed as

5-MethylcytosineArabidopsisArabidopsis ProteinsBase SequenceDNA GlycosylasesDNA PrimersModels, MolecularNuclear ProteinsPolymerase Chain ReactionSubstrate Specificity5-MethylcytosineArabidopsis ProteinsDNA GlycosylasesDNA PrimersNuclear ProteinsROS1 protein, Arabidopsis

Identifiers

PMID24678721
PMCPMC4004242
OpenAlexW2336801953

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

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.