Evidence map›Paper›PMID 24828757›Full record

ArticleBiochemistry2014

Unusual characteristics of the DNA binding domain of epigenetic regulatory protein MeCP2 determine its binding specificity.

Sergei Khrapunov, Christopher Warren, Huiyong Cheng, Esther R Berko, John M Greally, Michael Brenowitz

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 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
7.5field-weighted citation impact, top 2% 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

34 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Epigenetics in rare neurological diseases.Frontiers in cell and developmental biology · 2024
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. DNA Methylation and Adult Neurogenesis.Brain plasticity (Amsterdam, Netherlands) · 2017
    Review
  15. Review
  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

6 authors at 2 institutions in 1 country.

Sergei KhrapunovDepartment of Biochemistry and ‡Department of Genetics, Albert Einstein College of Medicine of Yeshiva University , 1300 Morris Park Avenue, Bronx, New York 10461, United States.
Christopher Warren
Huiyong Cheng
Esther R Berko
John M Greally
Michael Brenowitz
Albert Einstein College of Medicine · USYeshiva University · US

Funding

Translational Neuroimaging CoreP30HD071593 · NICHD · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI WALKLEY, STEVEN UPSHAW · 2011 to 2015
$5.6M
Principles of Protein Mimicry of DNAR01GM079618 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI BRENOWITZ, MICHAEL D. · 2008 to 2011
$1.4M
NICHD NIH HHS P30 HD071593NIGMS NIH HHS 1R01-GM079618NIGMS NIH HHS R01 GM079618
6 · The paper itself

Abstract

The protein MeCP2 mediates epigenetic regulation by binding methyl-CpG (mCpG) sites on chromatin. MeCP2 consists of six domains of which one, the methyl binding domain (MBD), binds mCpG sites in duplex DNA. We show that solution conditions with physiological or greater salt concentrations or the presence of nonspecific competitor DNA is necessary for the MBD to discriminate mCpG from CpG with high specificity. The specificity for mCpG over CpG is >100-fold under these solution conditions. In contrast, the MBD does not discriminate hydroxymethyl-CpG from CpG. The MBD is unusual among site-specific DNA binding proteins in that (i) specificity is not conferred by the enhanced affinity for the specific site but rather by suppression of its affinity for generic DNA, (ii) its specific binding to mCpG is highly electrostatic, and (iii) it takes up as well as displaces monovalent cations upon DNA binding. The MBD displays an unusually high affinity for single-stranded DNA independent of modification or sequence. In addition, the MBD forms a discrete dimer on DNA via a noncooperative binding pathway. Because the affinity of the second monomer is 1 order of magnitude greater than that of nonspecific binding, the MBD dimer is a unique molecular complex. The significance of these results in the context of neuronal function and development and MeCP2-related developmental disorders such as Rett syndrome is discussed.

Indexed as

Epigenesis, GeneticCations, MonovalentCpG IslandsDimerizationDNADNA, Single-StrandedMethyl-CpG-Binding Protein 2OligonucleotidesProtein BindingProtein Structure, TertiarySaltsSolutionsStatic ElectricityThermodynamicsCations, MonovalentDNADNA, Single-StrandedMethyl-CpG-Binding Protein 2OligonucleotidesSaltsSolutions

Identifiers

PMID24828757
PMCPMC4045320
OpenAlexW2322858711

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.