Evidence map›Paper›PMID 36468865›Full record

ArticlemSphere2022

Previously Unidentified Histone H1-Like Protein Is Involved in Cell Division and Ribosome Biosynthesis in Toxoplasma gondii.

Vanessa Severo, Rodolpho Souza, Francisca Vitorino, Julia Cunha, Andréa Ávila, Gustavo Arrizabalaga, Sheila Nardelli

Open access · goldAbstract read
In one paragraph

Article in mSphere, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

4 citing papers in PubMed, 10 citations in OpenAlex.

  1. Atlas ofeLife · 2023
    Article
  2. Atlas ofbioRxiv : the preprint server for biology · 2023
    Article
  3. Article
  4. Histone variant H2B.Z acetylation is necessary for maintenance ofbioRxiv : the preprint server for biology · 2023
    Article
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 3 institutions in 2 countries.

Vanessa SeveroLaboratório de Pesquisa em Apicomplexa, Instituto Carlos Chagas-FIOCRUZ/PR, Curitiba, Paraná, Brazil.ORCID 0000-0002-7095-1325
Rodolpho SouzaDepartment of Pharmacology and Toxicology, Indiana University School of Medicine, Indianapolis, Indiana, USA.
Francisca VitorinoLaboratório de Ciclo Celular, Instituto Butantan, São Paulo, Brazil.
Julia CunhaLaboratório de Ciclo Celular, Instituto Butantan, São Paulo, Brazil.
Andréa ÁvilaLaboratório de Pesquisa em Apicomplexa, Instituto Carlos Chagas-FIOCRUZ/PR, Curitiba, Paraná, Brazil.ORCID 0000-0001-5221-261X
Gustavo ArrizabalagaDepartment of Pharmacology and Toxicology, Indiana University School of Medicine, Indianapolis, Indiana, USA.ORCID 0000-0002-4445-0375
Sheila NardelliLaboratório de Pesquisa em Apicomplexa, Instituto Carlos Chagas-FIOCRUZ/PR, Curitiba, Paraná, Brazil.ORCID 0000-0002-1387-8096
Fundação Carlos Chagas · BRIndiana University School of MedicineInstituto Butantan · BR

Funding

Dissecting the calcium dependent phosphorylation network of Toxoplasma gondiiR01AI123457 · NIAID · INDIANA UNIVERSITY INDIANAPOLIS · PI ARRIZABALAGA, GUSTAVO A, TREECK, MORITZ · 2016 to 2020
$2.7M
Interleukin-1 and Steroid Signaling Drive Toxoplasma-induced Prostatic HyperplasiaR01DK124067 · NIDDK · INDIANA UNIVERSITY INDIANAPOLIS · PI ARRIZABALAGA, GUSTAVO A, JERDE, TRAVIS J · 2020 to 2023
$2.1M
Regulation of mitochondrial morphodynamics in Toxoplasma gondiiR01AI149766 · NIAID · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI ARRIZABALAGA, GUSTAVO A · 2020 to 2024
$2.0M
Homologs of brassinosteroid signaling proteins in Toxoplasma gondii regulate parasite divisionR21AI164619 · NIAID · INDIANA UNIVERSITY INDIANAPOLIS · PI ARRIZABALAGA, GUSTAVO A · 2021 to 2022
$436k
NIAID NIH HHS R01 AI123457NIAID NIH HHS R01 AI149766NIAID NIH HHS R21 AI164619NIDDK NIH HHS R01 DK124067
6 · The paper itself

Abstract

Chromatin dynamics can regulate all DNA-dependent processes. Access to DNA within chromatin is orchestrated mainly by histones and their posttranslational modifications (PTMs). Like other eukaryotes, the apicomplexan parasite Toxoplasma gondii encodes four canonical histones and five histone variants. In contrast, the linker histone (H1) has never been identified in apicomplexan parasites. In other eukaryotes, histone H1 compacts the chromatin by linking the nucleosome and increasing the DNA compaction. H1 is a multifunctional protein and can be involved in different steps of DNA metabolism or associated with protein complexes related to distinct biological processes. We have identified a novel protein in T. gondii ("TgH1-like") that, although lacking the globular domain of mammalian H1, is remarkably like the H1-like proteins of bacteria and trypanosomatids. Our results demonstrate that TgH1-like is a nuclear protein associated with chromatin and other histones. Curiously, TgH1-like is also in the nucleolus and associated with ribosomal proteins, indicating a versatile function in this parasite. Although knockout of the

Indexed as

Biological PhenomenaToxoplasmaAnimalsCell DivisionChromatinDNAHistonesHumansMammalsNucleosomesRibosomesChromatinDNAHistonesNucleosomescell divisionchromatinhistone H1posttranslational modificationToxoplasma gondii

Identifiers

PMID36468865
PMCPMC9769792
OpenAlexW4310702101

What Socratic 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 Socratic graph.