Evidence map›Paper›PMID 23316048›Full record

ArticleThe Journal of biological chemistry2013

Structural basis of the versatile DNA recognition ability of the methyl-CpG binding domain of methyl-CpG binding domain protein 4.

Junji Otani, Kyohei Arita, Tsuyoshi Kato, Mariko Kinoshita, Hironobu Kimura, Isao Suetake, Shoji Tajima, Mariko Ariyoshi, Masahiro Shirakawa

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

45 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
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  3. 8-Oxoguanine: A Lesion, an Epigenetic Mark, or a Molecular Signal?International journal of molecular sciences · 2025
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  5. Prognostic Significance ofPhenomics (Cham, Switzerland) · 2024
    Article
  6. Article
  7. Micronutrient regulation of the DNA methylome.Frontiers in epigenetics and epigenomics · 2024
    Review
  8. Article
  9. Article
  10. Noncatalytic Domains in DNA Glycosylases.International journal of molecular sciences · 2022
    Review
  11. Article
  12. Proteins That Read DNA Methylation.Advances in experimental medicine and biology · 2022
    Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Detecting and interpreting DNA methylation marks.Current opinion in structural biology · 2018
    Review
  20. Zinc Finger Readers of Methylated DNA.Molecules (Basel, Switzerland) · 2018
    Review
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

9 authors at 3 institutions in 4 countries.

Junji OtaniGraduate School of Engineering, Kyoto University, Kyoto 615-8510, Japan.
Kyohei Arita
Tsuyoshi Kato
Mariko Kinoshita
Hironobu Kimura
Isao Suetake
Shoji Tajima
Mariko Ariyoshi
Masahiro Shirakawa
Kyoto University · JPProtein Research Foundation · JPRIKEN Center for Integrative Medical Sciences · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The methyl-CpG binding domain (MBD) protein MBD4 participates in DNA repair as a glycosylase that excises mismatched thymine bases in CpG sites and also functions in transcriptional repression. Unlike other MBD proteins, MBD4 recognizes not only methylated CpG dinucleotides ((5m)CG/(5m)CG) but also T/G mismatched sites generated by spontaneous deamination of 5-methylcytosine ((5m)CG/TG). The glycosylase activity of MBD4 is also implicated in active DNA demethylation initiated by the deaminase-catalyzed conversion of 5-methylcytosine to thymine. Here, we report the crystal structures of the MBD of MBD4 (MBDMBD4) complexed with (5m)CG/(5m)CG and (5m)CG/TG. The crystal structures show that the DNA interface of MBD4 has flexible structural features and harbors an extensive water network that supports its dual base specificities. Combined with the results of biochemical analyses, the crystal structure of MBD4 bound to 5-hydroxymethylcytosine further demonstrates that MBDMBD4 is able to recognize a wide range of 5-methylcytosine modifications through the unique water network. The versatile base recognition ability of MBDMBD4 implies multifunctional roles for MBD4 in the regulation of dynamic DNA methylation patterns coupled with deamination and/or oxidation of 5-methylcytosine.

Indexed as

5-MethylcytosineAnimalsCrystallography, X-RayCytosineDNA MethylationEndodeoxyribonucleasesHumansMiceProtein Structure, TertiaryStructure-Activity Relationship5-hydroxymethylcytosine5-MethylcytosineCytosineEndodeoxyribonucleasesMBD4 protein, humanMbd4 protein, mouse

Identifiers

PMID23316048
PMCPMC3585070
OpenAlexW1965991279

What OpenQuestion holds

Textmetadata
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.