Evidence map›Paper›PMID 19172748›Full record

ArticleNature structural & molecular biology2008

Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75.

Christopher E Berndsen, Toshiaki Tsubota, Scott E Lindner, Susan Lee, James M Holton, Paul D Kaufman, James L Keck, John M Denu

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

81 citing papers in PubMed, 112 citations in OpenAlex.

  1. HAT1 Regulates Intestinal Stem Cell Proliferation and Differentiation.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Catalysis by protein acetyltransferase Gcn5.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021
    Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

21 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

8 authors at 3 institutions in 1 country.

Christopher E BerndsenDepartment of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, 1300 University Avenue, Madison, Wisconsin 53706, USA.
Toshiaki Tsubota
Scott E Lindner
Susan Lee
James M Holton
Paul D Kaufman
James L Keck
John M Denu
University of Wisconsin–Madison · USUniversity of Massachusetts Chan Medical School · USLawrence Berkeley National Laboratory · US

Funding

Regulation of repetitive chromatin structures during the human cell cycleR01GM055712 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI KAUFMAN, PAUL D. · 1997 to 2014
$5.1M
Molecular mechanisms of histone modification - Alzheimer’s supplement NOT-AG-18-008R37GM059785 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI DENU, JOHN M · 2013 to 2022
$3.7M
Molecular Mechanisms of Histone AcetyltransferasesR01GM059785 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI DENU, JOHN M · 1999 to 2012
$2.9M
NIGMS NIH HHS GM055712NIGMS NIH HHS GM059785NIGMS NIH HHS R01 GM055712NIGMS NIH HHS R01 GM059785NIGMS NIH HHS R37 GM059785
6 · The paper itself

Abstract

Histone acetylation and nucleosome remodeling regulate DNA damage repair, replication and transcription. Rtt109, a recently discovered histone acetyltransferase (HAT) from Saccharomyces cerevisiae, functions with the histone chaperone Asf1 to acetylate lysine K56 on histone H3 (H3K56), a modification associated with newly synthesized histones. In vitro analysis of Rtt109 revealed that Vps75, a Nap1 family histone chaperone, could also stimulate Rtt109-dependent acetylation of H3K56. However, the molecular function of the Rtt109-Vps75 complex remains elusive. Here we have probed the molecular functions of Vps75 and the Rtt109-Vps75 complex through biochemical, structural and genetic means. We find that Vps75 stimulates the kcat of histone acetylation by approximately 100-fold relative to Rtt109 alone and enhances acetylation of K9 in the H3 histone tail. Consistent with the in vitro evidence, cells lacking Vps75 showed a substantial reduction (60%) in H3K9 acetylation during S phase. X-ray structural, biochemical and genetic analyses of Vps75 indicate a unique, structurally dynamic Nap1-like fold that suggests a potential mechanism of Vps75-dependent activation of Rttl09. Together, these data provide evidence for a multifunctional HAT-chaperone complex that acetylates histone H3 and deposits H3-H4 onto DNA, linking histone modification and nucleosome assembly.

Indexed as

Amino Acid SequenceAnimalsCatalytic DomainCrystallography, X-RayEnzyme ActivationHistone AcetyltransferasesHistonesIn Vitro TechniquesKineticsModels, MolecularMolecular ChaperonesMolecular Sequence DataMultiprotein ComplexesProtein Structure, TertiaryRecombinant ProteinsSaccharomyces cerevisiaeHistone AcetyltransferasesHistonesMolecular ChaperonesMultiprotein ComplexesRecombinant ProteinsRtt109 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsVps75 protein, S cerevisiaeXenopus Proteins

Identifiers

PMID19172748
PMCPMC2678805
OpenAlexW2049341559

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.