Evidence map›Paper›PMID 26951436›Full record

ArticlePlant physiology2016

The Histone Deacetylase Complex 1 Protein of Arabidopsis Has the Capacity to Interact with Multiple Proteins Including Histone 3-Binding Proteins and Histone 1 Variants.

Giorgio Perrella, Craig Carr, Maria A Asensi-Fabado, Naomi A Donald, Katalin Páldi, Matthew A Hannah, Anna Amtmann

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
10.3field-weighted citation impact, top 3% 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

17 citing papers in PubMed, 36 citations in OpenAlex.

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  15. Structural disorder in plant proteins: where plasticity meets sessility.Cellular and molecular life sciences : CMLS · 2017
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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

7 authors at 2 institutions in 2 countries.

Giorgio PerrellaPlant Science Group, MCSB, MVLS, University of Glasgow, Glasgow G12 8QQ, United Kingdom (G.P., C.C., M.A.A.-F., N.A.D., K.P., A.A.); andBayer CropScience, B-9052 Ghent, Belgium (M.A.H.).ORCID 0000-0001-8972-1733
Craig CarrPlant Science Group, MCSB, MVLS, University of Glasgow, Glasgow G12 8QQ, United Kingdom (G.P., C.C., M.A.A.-F., N.A.D., K.P., A.A.); andBayer CropScience, B-9052 Ghent, Belgium (M.A.H.).
Maria A Asensi-FabadoPlant Science Group, MCSB, MVLS, University of Glasgow, Glasgow G12 8QQ, United Kingdom (G.P., C.C., M.A.A.-F., N.A.D., K.P., A.A.); andBayer CropScience, B-9052 Ghent, Belgium (M.A.H.).
Naomi A DonaldPlant Science Group, MCSB, MVLS, University of Glasgow, Glasgow G12 8QQ, United Kingdom (G.P., C.C., M.A.A.-F., N.A.D., K.P., A.A.); andBayer CropScience, B-9052 Ghent, Belgium (M.A.H.).
Katalin PáldiPlant Science Group, MCSB, MVLS, University of Glasgow, Glasgow G12 8QQ, United Kingdom (G.P., C.C., M.A.A.-F., N.A.D., K.P., A.A.); andBayer CropScience, B-9052 Ghent, Belgium (M.A.H.).ORCID 0000-0002-2861-2266
Matthew A HannahPlant Science Group, MCSB, MVLS, University of Glasgow, Glasgow G12 8QQ, United Kingdom (G.P., C.C., M.A.A.-F., N.A.D., K.P., A.A.); andBayer CropScience, B-9052 Ghent, Belgium (M.A.H.).
Anna AmtmannPlant Science Group, MCSB, MVLS, University of Glasgow, Glasgow G12 8QQ, United Kingdom (G.P., C.C., M.A.A.-F., N.A.D., K.P., A.A.); andBayer CropScience, B-9052 Ghent, Belgium (M.A.H.) anna.amtmann@glasgow.ac.uk.
University of Glasgow · GBBayer (Belgium) · BE

Funding

Biotechnology and Biological Sciences Research Council BB/K008218/1
6 · The paper itself

Abstract

Intrinsically disordered proteins can adopt multiple conformations, thereby enabling interaction with a wide variety of partners. They often serve as hubs in protein interaction networks. We have previously shown that the Histone Deacetylase Complex 1 (HDC1) protein from Arabidopsis (Arabidopsis thaliana) interacts with histone deacetylases and quantitatively determines histone acetylation levels, transcriptional activity, and several phenotypes, including abscisic acid sensitivity during germination, vegetative growth rate, and flowering time. HDC1-type proteins are ubiquitous in plants, but they contain no known structural or functional domains. Here, we explored the protein interaction spectrum of HDC1 using a quantitative bimolecular fluorescence complementation assay in tobacco (Nicotiana benthamiana) epidermal cells. In addition to binding histone deacetylases, HDC1 directly interacted with histone H3-binding proteins and corepressor-associated proteins but not with H3 or the corepressors themselves. Surprisingly, HDC1 also was able to interact with variants of the linker histone H1. Truncation of HDC1 to the ancestral core sequence narrowed the spectrum of interactions and of phenotypic outputs but maintained binding to a H3-binding protein and to H1. Thus, HDC1 provides a potential link between H1 and histone-modifying complexes.

Indexed as

Protein Interaction MapsArabidopsisArabidopsis ProteinsCarrier ProteinsEscherichia coliFlowersGene Expression ProfilingGenetic VectorsGerminationHistone DeacetylasesHistonesMicroscopy, ConfocalNicotianaNuclear ProteinsPlants, Genetically ModifiedArabidopsis ProteinsCarrier ProteinsHDC1 protein, ArabidopsisHistone DeacetylasesHistonesNuclear Proteins

Identifiers

PMID26951436
PMCPMC4854681
OpenAlexW2294513735

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.