Evidence map›Paper›PMID 20974931›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Domain structure of the DEMETER 5-methylcytosine DNA glycosylase.

Young Geun Mok, Rie Uzawa, Jiyoon Lee, Gregory M Weiner, Brandt F Eichman, Robert L Fischer, Jin Hoe Huh

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

47 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Base Excision DNA Repair in Plants:International journal of molecular sciences · 2023
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Targeting Induced Local Lesions in the WheatFrontiers in nutrition · 2022
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Active DNA Demethylation in Plants.International journal of molecular sciences · 2019
    Review
  19. The catalytic core of DEMETER guides active DNA demethylation inProceedings of the National Academy of Sciences of the United States of America · 2019
    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

7 authors at 3 institutions in 2 countries.

Young Geun MokDepartment of Plant Science and Plant Genomics and Breeding Institute, Seoul National University, Seoul 151-921, Korea.
Rie Uzawa
Jiyoon Lee
Gregory M Weiner
Brandt F Eichman
Robert L Fischer
Jin Hoe Huh
Seoul National University · KRUniversity of California, Berkeley · USVanderbilt University · US

Funding

Regulation and Function of DNA Demethylation in ArabidopsisR01GM069415 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI FISCHER, ROBERT L, ZILBERMAN, DANIEL · 2004 to 2016
$3.8M
NIGMS NIH HHS R01 GM069415NIGMS NIH HHS R01-GM069415
6 · The paper itself

Abstract

DNA glycosylases initiate the base excision repair (BER) pathway by excising damaged, mismatched, or otherwise modified bases. Animals and plants independently evolved active BER-dependent DNA demethylation mechanisms important for epigenetic reprogramming. One such DNA demethylation mechanism is uniquely initiated in plants by DEMETER (DME)-class DNA glycosylases. Arabidopsis DME family glycosylases contain a conserved helix-hairpin-helix domain present in both prokaryotic and eukaryotic DNA glycosylases as well as two domains A and B of unknown function that are unique to this family. Here, we employed a mutagenesis approach to screen for DME residues critical for DNA glycosylase activity. This analysis revealed that amino acids clustered in all three domains, but not in the intervening variable regions, are required for in vitro 5-methylcytosine excision activity. Amino acids in domain A were found to be required for nonspecific DNA binding, a prerequisite for 5-methylcytosine excision. In addition, mutational analysis confirmed the importance of the iron-sulfur cluster motif to base excision activity. Thus, the DME DNA glycosylase has a unique structure composed of three essential domains that all function in 5-methylcytosine excision.

Indexed as

DNA Repair5-MethylcytosineAmino AcidsArabidopsisArabidopsis ProteinsDNA GlycosylasesDNA MethylationIron-Sulfur ProteinsMutagenesis, Site-DirectedProtein Structure, Tertiary5-MethylcytosineAmino AcidsArabidopsis ProteinsDNA GlycosylasesIron-Sulfur Proteins

Identifiers

PMID20974931
PMCPMC2984145
OpenAlexW2080335963

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.