Evidence map›Paper›PMID 16543219›Full record

ArticleGenes & development2006

The Saccharomyces cerevisiae histone H2A variant Htz1 is acetylated by NuA4.

Michael-Christopher Keogh, Thomas A Mennella, Chika Sawa, Sharon Berthelet, Nevan J Krogan, Adam Wolek, Vladimir Podolny, Laura Rocco Carpenter, Jack F Greenblatt, Kristin Baetz and 1 more

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 149 papers.

0numbers the graph read from it
0cells of the map it votes in
149citing papers in PubMed
–field-weighted citation impact
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

149 citing papers in PubMed, 234 citations in OpenAlex.

  1. Article
  2. Review
  3. Cryo-EM structures reveal the acetylation process of piccolo NuA4.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Frontiers in epigenetics and epigenomics · 2024
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Structure of the NuA4 histone acetyltransferase complex.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

89 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

11 authors at 5 institutions in 2 countries.

Michael-Christopher KeoghDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Thomas A Mennella
Chika Sawa
Sharon Berthelet
Nevan J Krogan
Adam Wolek
Vladimir Podolny
Laura Rocco Carpenter
Jack F Greenblatt
Kristin Baetz
Stephen Buratowski
Harvard University · USUniversity of Ottawa · CAUpstate Freshwater Institute · USUniversity of California, San Francisco · USUniversity of Toronto · CA

Funding

The RNA polymerase II transcription complexR01GM046498 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI BURATOWSKI, STEPHEN · 1996 to 2024
$9.4M
RNA POLYMERASE II TRANSCRIPTION INITIATION COMPLEXR29GM046498 · NIGMS · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI BURATOWSKI, STEPHEN · 1991 to 1995
–
NIGMS NIH HHS GM46498NIGMS NIH HHS R01 GM046498
6 · The paper itself

Abstract

The histone H2A variant H2A.Z (Saccharomyces cerevisiae Htz1) plays roles in transcription, DNA repair, chromosome stability, and limiting telomeric silencing. The Swr1-Complex (SWR-C) inserts Htz1 into chromatin and shares several subunits with the NuA4 histone acetyltransferase. Furthermore, mutants of these two complexes share several phenotypes, suggesting they may work together. Here we show that NuA4 acetylates Htz1 Lys 14 (K14) after the histone is assembled into chromatin by the SWR-C. K14 mutants exhibit specific defects in chromosome transmission without affecting transcription, telomeric silencing, or DNA repair. Function-specific modifications may help explain how the same component of chromatin can function in diverse pathways.

Indexed as

AcetylationAcetyltransferasesAmino Acid SequenceChromosomes, FungalHistone AcetyltransferasesHistonesMolecular Sequence DataSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidAcetyltransferasesHistone AcetyltransferasesHistonesHtz1 protein, S cerevisiaeNuA4 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID16543219
PMCPMC1413285
OpenAlexW2160025279

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.