Evidence map›Paper›PMID 16543222›Full record

ArticleGenes & development2006

Telomeric heterochromatin boundaries require NuA4-dependent acetylation of histone variant H2A.Z in Saccharomyces cerevisiae.

Joshua E Babiarz, Jeffrey E Halley, Jasper Rine

Abstract 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 128 papers.

0numbers the graph read from it
0cells of the map it votes in
128citing 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

128 citing papers in PubMed.

  1. Article
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  4. Cryo-EM structures reveal the acetylation process of piccolo NuA4.Proceedings of the National Academy of Sciences of the United States of America · 2025
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68 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

3 authors.

Joshua E BabiarzDepartment of Molecular and Cell Biology, University of California at Berkeley, Berkeley, California 94720-3202, USA.
Jeffrey E Halley
Jasper Rine

Funding

THE MOLECULAR BASIS OF CELL FUNCTIONT32GM007232 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BILDER, DAVID, UNAL, ELCIN · 1985 to 2022
$36.4M
GENETIC ANALYSIS OF THE GENES CONTROLLING A POSITIONR01GM031105 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI RINE, JASPER D · 1985 to 2020
$6.4M
GENETIC ANALYSIS OF GENES CONTROLLING A POSITION EFFECTR37GM031105 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI RINE, JASPER D · 1999 to 2008
$3.5M
STUDIES OF ENVIRONMENTAL MUTAGENS AND CARCINOGENST32ES007075 · NIEHS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BJELDANES, LEONARD F · 1985 to 2004
$865k
NIEHS NIH HHS 5 T32 ES07075NIEHS NIH HHS T32 ES007075NIGMS NIH HHS 5 T32 GM07232NIGMS NIH HHS GM31105NIGMS NIH HHS R01 GM031105NIGMS NIH HHS R37 GM031105NIGMS NIH HHS T32 GM007232
6 · The paper itself

Abstract

SWR1-Com, which is responsible for depositing H2A.Z into chromatin, shares four subunits with the NuA4 histone acetyltransferase complex. This overlap in composition led us to test whether H2A.Z was a substrate of NuA4 in vitro and in vivo. The N-terminal tail of H2A.Z was acetylated in vivo at multiple sites by a combination of NuA4 and SAGA. H2A.Z acetylation was also dependent on SWR1-Com, causing H2A.Z to be efficiently acetylated only when incorporated in chromatin. Unacetylatable H2A.Z mutants were, like wild-type H2A.Z, enriched at heterochromatin boundaries, but were unable to block spreading of heterochromatin. A mutant version of H2A.Z that could not be acetylated, in combination with a mutation in a nonessential gene in the NuA4 complex, caused a pronounced decrease in growth rate. This H2A.Z mutation was lethal in combination with a mutant version of histone H4 that could not be acetylated by NuA4. Taken together, these results show a role for H2A.Z acetylation in restricting silent chromatin, and reveal that acetylation of H2A.Z and H4 can contribute to a common function essential to life.

Indexed as

TelomereAcetylationAcetyltransferasesGene SilencingHeterochromatinHistone AcetyltransferasesHistonesPolymerase Chain ReactionSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAcetyltransferasesHeterochromatinHistone AcetyltransferasesHistonesHtz1 protein, S cerevisiaeNuA4 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID16543222
PMCPMC1413290

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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.