Evidence map›Paper›PMID 21094070›Full record

ArticleMolecular cell2010

Structure and biological importance of the Spn1-Spt6 interaction, and its regulatory role in nucleosome binding.

Seth M McDonald, Devin Close, Hua Xin, Tim Formosa, Christopher P Hill

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

60 citing papers in PubMed, 89 citations in OpenAlex.

  1. Article
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  10. Article
  11. Review
  12. Toward structural understanding of eukaryotic transcription elongation.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2025
    Review
  13. Article
  14. Chromatin regulates alternative polyadenylation via the RNA polymerase II elongation rate.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Review
  20. The Histone Chaperone Network Is Highly Conserved inInternational journal of molecular sciences · 2023
    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

5 authors at 1 institution in 1 country.

Seth M McDonaldDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112-5650, USA.
Devin Close
Hua Xin
Tim Formosa
Christopher P Hill
University of Utah · US

Funding

Nucleosome Reorganizing/Remodeling ComplexesR01GM076242 · NIGMS · UNIVERSITY OF UTAH · PI HILL, CHRISTOPHER P. · 2006 to 2013
$2.2M
NIGMS NIH HHS R01 GM076242
6 · The paper itself

Abstract

Eukaryotic transcription and mRNA processing depend upon the coordinated interactions of many proteins, including Spn1 and Spt6, which are conserved across eukaryotes, are essential for viability, and associate with each other in some of their biologically important contexts. Here we report crystal structures of the Spn1 core alone and in complex with the binding determinant of Spt6. Mutating interface residues greatly diminishes binding in vitro and causes strong phenotypes in vivo, including a defect in maintaining repressive chromatin. Overexpression of Spn1 partially suppresses the defects caused by an spt6 mutation affecting the Spn1 interface, indicating that the Spn1-Spt6 interaction is important for managing chromatin. Spt6 binds nucleosomes directly in vitro, and this interaction is blocked by Spn1, providing further mechanistic insight into the function of the interaction. These data thereby reveal the structural and biochemical bases of molecular interactions that function in the maintenance of chromatin structure.

Indexed as

Amino Acid SequenceHistone ChaperonesModels, MolecularMolecular Sequence DataMutationNuclear ProteinsNucleosomesRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscriptional Elongation FactorsHistone ChaperonesNuclear ProteinsNucleosomesRNA, MessengerSaccharomyces cerevisiae ProteinsSPN1 protein, S cerevisiaeSPT6 protein, S cerevisiaeTranscriptional Elongation Factors

Identifiers

PMID21094070
PMCPMC3017428
OpenAlexW1968153105

What OpenQuestion holds

Textmetadata
LicenceTDM
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.