Evidence map›Paper›PMID 29463645›Full record

ArticleMolecular and cellular biology2018

Molecular Architecture of the Essential Yeast Histone Acetyltransferase Complex NuA4 Redefines Its Multimodularity.

Dheva Setiaputra, Salar Ahmad, Udit Dalwadi, Anne-Lise Steunou, Shan Lu, James D Ross, Meng-Qiu Dong, Jacques Côté, Calvin K Yip

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

20 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
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  3. Structure of the human TIP60 complex.Nature communications · 2024
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  5. Article
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  7. The NuA4 histone acetyltransferase: variations on a theme of SAGA.Nature structural & molecular biology · 2023
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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

9 authors at 3 institutions in 2 countries.

Dheva SetiaputraDepartment of Biochemistry and Molecular Biology, The University of British Columbia, Vancouver, British Columbia, Canada.
Salar AhmadSt-Patrick Research Group in Basic Oncology, Laval University Cancer Research Center, Oncology Axis-CHU de Québec-UL Research Center, Quebec City, Quebec, Canada.
Udit DalwadiDepartment of Biochemistry and Molecular Biology, The University of British Columbia, Vancouver, British Columbia, Canada.
Anne-Lise SteunouSt-Patrick Research Group in Basic Oncology, Laval University Cancer Research Center, Oncology Axis-CHU de Québec-UL Research Center, Quebec City, Quebec, Canada.
Shan LuNational Institute of Biological Sciences, Beijing, Beijing, China.
James D RossDepartment of Biochemistry and Molecular Biology, The University of British Columbia, Vancouver, British Columbia, Canada.
Meng-Qiu DongNational Institute of Biological Sciences, Beijing, Beijing, China.
Jacques CôtéSt-Patrick Research Group in Basic Oncology, Laval University Cancer Research Center, Oncology Axis-CHU de Québec-UL Research Center, Quebec City, Quebec, Canada.ORCID 0000-0001-6751-555X
Calvin K YipDepartment of Biochemistry and Molecular Biology, The University of British Columbia, Vancouver, British Columbia, Canada calvin.yip@ubc.ca.ORCID 0000-0003-1779-9501
University of British Columbia · CAUniversité Laval · CANational Institute of Biological Sciences, Beijing · CN

Funding

CIHR FDN-143228CIHR FDN-143314
6 · The paper itself

Abstract

Conserved from yeast to humans, the NuA4 histone acetyltransferase is a large multisubunit complex essential for cell viability through the regulation of gene expression, genome maintenance, metabolism, and cell fate during development and stress. How the different NuA4 subunits work in concert with one another to perform these diverse functions remains unclear, and addressing this central question requires a comprehensive understanding of NuA4's molecular architecture and subunit organization. We have determined the structure of fully assembled native yeast NuA4 by single-particle electron microscopy. Our data revealed that NuA4 adopts a trilobal overall architecture, with each of the three lobes constituted by one or two functional modules. By performing cross-linking coupled to mass spectrometry analysis and

Indexed as

AcetylationAmino Acid SequenceHistone AcetyltransferasesHistonesMicroscopy, ElectronNucleosomesProtein SubunitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsHistone AcetyltransferasesHistonesNuA4 protein, S cerevisiaeNucleosomesProtein SubunitsSaccharomyces cerevisiae Proteinscross-linking coupled to mass spectrometryelectron microscopyhistone acetyltransferaseNuA4yeast

Identifiers

PMID29463645
PMCPMC5902594
OpenAlexW2790771181

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.