Evidence map›Paper›PMID 19696079›Full record

ArticleNucleic acids research2009

Cooperative action of TIP48 and TIP49 in H2A.Z exchange catalyzed by acetylation of nucleosomal H2A.

Jongkyu Choi, Kyu Heo, Woojin An

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

43 citing papers in PubMed, 67 citations in OpenAlex.

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  13. The histone variant H2A.Z in gene regulation.Epigenetics & chromatin · 2019
    Review
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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

3 authors at 1 institution in 1 country.

Jongkyu ChoiDepartment of Biochemistry and Molecular Biology, University of Southern California, Norris Comprehensive Cancer Center, Los Angeles, CA 90033, USA.
Kyu Heo
Woojin An
University of Southern California · US

Funding

ROLE OF HISTONE H4 N-TERMINAL TAIL IN TRANSCRIPTION REGULATIONR01GM084209 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI AN, WOOJIN · 2008 to 2012
$1.8M
NIGMS NIH HHS R01 GM084209NIGMS NIH HHS R01GM84209
6 · The paper itself

Abstract

H2A.Z is an evolutionarily conserved H2A variant that plays a key role in the regulation of chromatin transcription. To understand the molecular mechanism of H2A.Z exchange, we purified two distinct H2A.Z-interacting complexes termed the small and big complexes from a human cell line. The big complex contains most components of the SRCAP chromatin remodeling and TIP60 HAT complexes, whereas the small complex possesses only a subset of SRCAP and TIP60 subunits. Our exchange analysis revealed that both small and big complexes enhance the incorporation of H2A.Z-H2B dimer into the nucleosome. In addition, TIP60-mediated acetylation of nucleosomal H2A specifically facilitates the action of the small complex in the H2A.Z exchange reaction. Among factors present in the small complex, we determined that TIP48 and TIP49 play a major role in catalyzing H2A acetylation-induced H2A.Z exchange via their ATPase activities. Overall, our work uncovers the previously-unrecognized role of TIP48 and TIP49 in H2A.Z exchange and a novel epigenetic mechanism controlling this process.

Indexed as

AcetylationAdenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesCarrier ProteinsCatalysisChromatinDNA HelicasesEpigenesis, GeneticHeLa CellsHistone AcetyltransferasesHistonesHumansLysine Acetyltransferase 5NucleosomesProtein SubunitsAdenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesCarrier ProteinsChromatinDNA HelicasesHistone Acetyltransferaseshistone H2A.F-ZHistonesKAT5 protein, humanLysine Acetyltransferase 5NucleosomesProtein SubunitsRUVBL1 protein, humanRUVBL2 protein, humanSRCAP protein, human

Identifiers

PMID19696079
PMCPMC2764430
OpenAlexW2032816715

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.