Evidence map›Paper›PMID 30796450›Full record

ArticleMolecular biology and evolution2019

Proteomic Analysis of Histones H2A/H2B and Variant Hv1 in Tetrahymena thermophila Reveals an Ancient Network of Chaperones.

Kanwal Ashraf, Syed Nabeel-Shah, Jyoti Garg, Alejandro Saettone, Joanna Derynck, Anne-Claude Gingras, Jean-Philippe Lambert, Ronald E Pearlman, Jeffrey Fillingham

Open access · hybridAbstract read
In one paragraph

Article in Molecular biology and evolution, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

13 citing papers in PubMed, 20 citations in OpenAlex.

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  11. Exploring the Histone Acetylation Cycle in the Protozoan ModelFrontiers in cell and developmental biology · 2020
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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 5 institutions in 1 country.

Kanwal AshrafDepartment of Biology, York University, Toronto, ON, Canada.
Syed Nabeel-ShahDepartment of Chemistry and Biology, Ryerson University, Toronto, ON, Canada.
Jyoti GargDepartment of Biology, York University, Toronto, ON, Canada.
Alejandro SaettoneDepartment of Chemistry and Biology, Ryerson University, Toronto, ON, Canada.
Joanna DerynckDepartment of Chemistry and Biology, Ryerson University, Toronto, ON, Canada.
Anne-Claude GingrasDepartment of Molecular Genetics, University of Toronto, Toronto, ON, Canada.
Jean-Philippe LambertDepartment of Molecular Medicine and Cancer Research Centre, Université Laval, Québec, QC, Canada.
Ronald E PearlmanDepartment of Biology, York University, Toronto, ON, Canada.
Jeffrey FillinghamDepartment of Chemistry and Biology, Ryerson University, Toronto, ON, Canada.
Toronto Metropolitan University · CAYork University · CACentre hospitalier universitaire de Québec · CALunenfeld-Tanenbaum Research Institute · CAUniversity of Toronto · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Epigenetic information, which can be passed on independently of the DNA sequence, is stored in part in the form of histone posttranslational modifications and specific histone variants. Although complexes necessary for deposition have been identified for canonical and variant histones, information regarding the chromatin assembly pathways outside of the Opisthokonts remains limited. Tetrahymena thermophila, a ciliated protozoan, is particularly suitable to study and unravel the chromatin regulatory layers due to its unique physical separation of chromatin states in the form of two distinct nuclei present within the same cell. Using a functional proteomics pipeline, we carried out affinity purification followed by mass spectrometry of endogenously tagged T. thermophila histones H2A, H2B and variant Hv1.We identified a set of interacting proteins shared among the three analyzed histones that includes the FACT-complex, as well as H2A- or Hv1-specific chaperones. We find that putative subunits of T. thermophila versions of SWR- and INO80-complexes, as well as transcription-related histone chaperone Spt6Tt specifically copurify with Hv1. We also identified importin β6 and the T. thermophila ortholog of nucleoplasmin 1 (cNpl1Tt) as H2A-H2B interacting partners. Our results further implicate Poly [ADP-ribose] polymerases in histone metabolism. Molecular evolutionary analysis, reciprocal affinity purification coupled to mass spectrometry experiments, and indirect immunofluorescence studies using endogenously tagged Spt16Tt (FACT-complex subunit), cNpl1Tt, and PARP6Tt underscore the validity of our approach and offer mechanistic insights. Our results reveal a highly conserved regulatory network for H2A (Hv1)-H2B concerning their nuclear import and assembly into chromatin.

Indexed as

Evolution, MolecularAmino Acid SequenceHistone ChaperonesHistonesPhylogenyPoly(ADP-ribose) PolymerasesProteomeProteomicsTetrahymena thermophilaHistone ChaperonesHistonesPoly(ADP-ribose) PolymerasesProteomeFACThistonehistone chaperonehistone H2Ahistone H2B

Identifiers

PMID30796450
PMCPMC6502085
OpenAlexW2917304564

What OpenQuestion holds

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Registered trials

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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.