Evidence map›Paper›PMID 14555760›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

Methylated DNA-binding domain 1 and methylpurine-DNA glycosylase link transcriptional repression and DNA repair in chromatin.

Sugiko Watanabe, Takaya Ichimura, Naoyuki Fujita, Shu Tsuruzoe, Izuru Ohki, Masahiro Shirakawa, Michio Kawasuji, Mitsuyoshi Nakao

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

37 citing papers in PubMed, 77 citations in OpenAlex.

  1. Review
  2. Article
  3. A DNA repair-independent role for alkyladenine DNA glycosylase in alkylation-induced unfolded protein response.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  4. Article
  5. Article
  6. Dynamic features of human mitochondrial DNA maintenance and transcription.Frontiers in cell and developmental biology · 2022
    Review
  7. Review
  8. Article
  9. Article
  10. DNA Methylation and Adult Neurogenesis.Brain plasticity (Amsterdam, Netherlands) · 2017
    Review
  11. Review
  12. Review
  13. Review
  14. An epigenetic regulator: methyl-CpG-binding domain protein 1 (MBD1).International journal of molecular sciences · 2015
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

8 authors at 2 institutions in 1 country.

Sugiko WatanabeDepartment of Regeneration Medicine, Institute of Molecular Embryology and Genetics, Kumamoto University, 2-2-1 Honjo, Kumamoto 860-0811, Japan.
Takaya Ichimura
Naoyuki Fujita
Shu Tsuruzoe
Izuru Ohki
Masahiro Shirakawa
Michio Kawasuji
Mitsuyoshi Nakao
Kumamoto University · JPYokohama City University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The methyl-CpG dinucleotide containing a symmetrical 5-methylcytosine (mC) is involved in gene regulation and genome stability. We report here that methylation-mediated transcriptional repressor methylated DNA-binding domain 1 (MBD1) interacts with methylpurine-DNA glycosylase (MPG), which excises damaged bases from substrate DNA. MPG itself actively represses transcription and has a synergistic effect on gene silencing together with MBD1. Chromatin immunoprecipitation analysis reveals the molecular movement of MBD1 and MPG in vivo: (i) The MBD1-MPG complex normally exists on the methylated gene promoter; (ii) treatment of cells with alkylating agent methylmethanesulfonate (MMS) induces the dissociation of MBD1 from the methylated promoter, and MPG is located on both methylated and unmethylated promoters; and (iii) after completion of the repair, the MBD1-MPG complex is restored on the methylated promoter. Mobility-shift and structural analyses show that the MBD of MBD1 binds a methyl-CpG pair (mCpG x mCpG) but not the methyl-CpG pair containing a single 7-methylguanine (N) (mCpG x mCpN) that is known as one of the major lesions caused by MMS. We further demonstrate that knockdown of MBD1 by specific small interfering RNAs significantly increases cell sensitivity to MMS. These data suggest that MBD1 cooperates with MPG for transcriptional repression and DNA repair. We hypothesize that MBD1 functions as a reservoir for MPG and senses the base damage in chromatin

Indexed as

DNA MethylationTranscription, GeneticBase SequenceBinding SitesChromatinCross-Linking ReagentsDinucleoside PhosphatesDNA GlycosylasesDNA, NeoplasmDNA RepairGene Expression Regulation, NeoplasticGlutathione TransferaseHeLa CellsHumansPlasmidsRecombinant Fusion ProteinsChromatinCpG dinucleotideCross-Linking ReagentsDinucleoside PhosphatesDNA GlycosylasesDNA, NeoplasmGlutathione TransferaseRecombinant Fusion ProteinsRNA, Small Interfering

Identifiers

PMID14555760
PMCPMC240709
OpenAlexW2103881488

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.