Evidence map›Paper›PMID 17880717›Full record

ArticleBMC biology2007

Association with the origin recognition complex suggests a novel role for histone acetyltransferase Hat1p/Hat2p.

Bernhard Suter, Oxana Pogoutse, Xinghua Guo, Nevan Krogan, Peter Lewis, Jack F Greenblatt, Jasper Rine, Andrew Emili

Open access · goldAbstract read
In one paragraph

Article in BMC biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

30 citing papers in PubMed, 49 citations in OpenAlex.

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  6. Recent insights intoEpigenetics · 2021
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  16. Structural basis for substrate specificity and catalysis of human histone acetyltransferase 1.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
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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 2 countries.

Bernhard SuterProgram in Proteomics and Bioinformatics, Banting and Best Department of Medical Genetics, University of Toronto, Toronto, Ontario, Canada. bernhard.suter@utoronto.ca
Oxana Pogoutse
Xinghua Guo
Nevan Krogan
Peter Lewis
Jack F Greenblatt
Jasper Rine
Andrew Emili
University of Toronto · CAUniversity of California, Berkeley · USUniversity of California, San Francisco · US

Funding

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
NIGMS NIH HHS GM31105NIGMS NIH HHS R01 GM031105NIGMS NIH HHS R37 GM031105
6 · The paper itself

Abstract

backgroundHistone modifications have been implicated in the regulation of transcription and, more recently, in DNA replication and repair. In yeast, a major conserved histone acetyltransferase, Hat1p, preferentially acetylates lysine residues 5 and 12 on histone H4.

resultsHere, we report that a nuclear sub-complex consisting of Hat1p and its partner Hat2p interacts physically and functionally with the origin recognition complex (ORC). While mutational inactivation of the histone acetyltransferase (HAT) gene HAT1 alone does not compromise origin firing or initiation of DNA replication, a deletion in HAT1 (or HAT2) exacerbates the growth defects of conditional orc-ts mutants. Thus, the ORC-associated Hat1p-dependent histone acetyltransferase activity suggests a novel linkage between histone modification and DNA replication. Additional genetic and biochemical evidence points to the existence of partly overlapping histone H3 acetyltransferase activities in addition to Hat1p/Hat2p for proper DNA replication efficiency. Furthermore, we demonstrated a dynamic association of Hat1p with chromatin during S-phase that suggests a role of this enzyme at the replication fork.

conclusionWe have found an intriguing new association of the Hat1p-dependent histone acetyltransferase in addition to its previously known role in nuclear chromatin assembly (Hat1p/Hat2p-Hif1p). The participation of a distinct Hat1p/Hat2p sub-complex suggests a linkage of histone H4 modification with ORC-dependent DNA replication.

Indexed as

DNA ReplicationAcetylationAcetyltransferasesAllelesBlotting, WesternChromatin ImmunoprecipitationDNA, FungalGene Expression Regulation, FungalGenes, FungalHistone AcetyltransferasesHistonesLysineMutationOpen Reading FramesOrigin Recognition ComplexSaccharomyces cerevisiaeAcetyltransferasesDNA, FungalHistone Acetyltransferaseshistone acetyltransferase type B complexHistonesLysineOrigin Recognition ComplexSaccharomyces cerevisiae Proteins

Identifiers

PMID17880717
PMCPMC2140264
OpenAlexW2004275075

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.