Evidence map›Paper›PMID 14739929›Full record

ArticleThe EMBO journal2004

Crystal structures of histone Sin mutant nucleosomes reveal altered protein-DNA interactions.

Uma M Muthurajan, Yunhe Bao, Lawrence J Forsberg, Rajeswari S Edayathumangalam, Pamela N Dyer, Cindy L White, Karolin Luger

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

80 citing papers in PubMed, 130 citations in OpenAlex.

  1. Review
  2. Article
  3. DNA Repair in Nucleosomes: Insights from Histone Modifications and Mutants.International journal of molecular sciences · 2024
    Review
  4. Review
  5. Histone mutations in cancer.Biochemical Society transactions · 2023
    Article
  6. Article
  7. TGM2-mediated histone transglutamination is dictated by steric accessibility.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Matching protein surface structural patches for high-resolution blind peptide docking.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. SMOG 2 and OpenSMOG: Extending the limits of structure-based models.Protein science : a publication of the Protein Society · 2022
    Article
  10. Article
  11. Structural studies of functional nucleosome complexes with transacting factors.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2022
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

20 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

Uma M MuthurajanDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, USA.
Yunhe Bao
Lawrence J Forsberg
Rajeswari S Edayathumangalam
Pamela N Dyer
Cindy L White
Karolin Luger
Colorado State University · US

Funding

Structure of nucleosomes in complex with transcriptional regulatorsR01GM061909 · NIGMS · COLORADO STATE UNIVERSITY-FORT COLLINS · PI LUGER, KAROLIN · 2000 to 2009
$2.0M
NIGMS NIH HHS GM61909NIGMS NIH HHS R01 GM061909
6 · The paper itself

Abstract

Here we describe 11 crystal structures of nucleosome core particles containing individual point mutations in the structured regions of histones H3 and H4. The mutated residues are located at the two protein-DNA interfaces flanking the nucleosomal dyad. Five of the mutations partially restore the in vivo effects of SWI/SNF inactivation in yeast. We find that even nonconservative mutations of these residues (which exhibit a distinct phenotype in vivo) have only moderate effects on global nucleosome structure. Rather, local protein-DNA interactions are disrupted and weakened in a subtle and complex manner. The number of lost protein-DNA interactions correlates directly with an increased propensity of the histone octamer to reposition with respect to the DNA, and with an overall destabilization of the nucleosome. Thus, the disruption of only two to six of the approximately 120 direct histone-DNA interactions within the nucleosome has a pronounced effect on nucleosome mobility and stability. This has implications for our understanding of how these structures are made accessible to the transcription and replication machinery in vivo.

Indexed as

Models, MolecularChromatinCrystallography, X-RayDNAHistonesHot TemperatureMagnesiumMotionNucleosomesPoint MutationProtein ConformationSodium ChlorideChromatinDNAHistonesMagnesiumNucleosomesSodium Chloride

Identifiers

PMID14739929
PMCPMC1271754
OpenAlexW1966667302

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.