Evidence map›Paper›PMID 16339723›Full record

ArticleEukaryotic cell2005

MYST family histone acetyltransferases in the protozoan parasite Toxoplasma gondii.

Aaron T Smith, Samantha D Tucker-Samaras, Alan H Fairlamb, William J Sullivan

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

25 citing papers in PubMed, 49 citations in OpenAlex.

  1. Analysis of the role of acetylation inFrontiers in microbiology · 2024
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Toxoplasma histone acetylation remodelers as novel drug targets.Expert review of anti-infective therapy · 2012
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. A decade of epigenetic research in Toxoplasma gondii.Molecular and biochemical parasitology · 2010
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

4 authors at 3 institutions in 2 countries.

Aaron T SmithDepartment of Pharmacology and Toxicology, Indiana University School of Medicine, 635 Barnhill Drive, Medical Sciences Building Room A-525, Indianapolis, IN 46202-5120, USA.
Samantha D Tucker-Samaras
Alan H Fairlamb
William J Sullivan
Wellcome Trust · GBIndiana University – Purdue University Indianapolis · USIndiana University School of Medicine

Funding

Production of New Adenovector Constructs with Fiber-Shaft ModificationsZ01AI005093 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI WALLACE, KIMBERLY · 2007 to 2008
$2.7M
GCN5-mediated transcription in AIDS pathogen ToxoplasmaR01GM065051 · NIGMS · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI SULLIVAN, WILLIAM J · 2003 to 2007
$1.2M
Intramural NIH HHS Z01 AI005093NIAID NIH HHS AI05093NIGMS NIH HHS GM065051NIGMS NIH HHS R01 GM065051Wellcome Trust
6 · The paper itself

Abstract

The restructuring of chromatin precedes tightly regulated events such as DNA transcription, replication, and repair. One type of chromatin remodeling involves the covalent modification of nucleosomes by histone acetyltransferase (HAT) complexes. The observation that apicidin exerts antiprotozoal activity by targeting a histone deacetyltransferase has prompted our search for more components of the histone modifying machinery in parasitic protozoa. We have previously identified GNAT family HATs in the opportunistic pathogen Toxoplasma gondii and now describe the first MYST (named for members MOZ, Ybf2/Sas3, Sas2, and Tip60) family HATs in apicomplexa (TgMYST-A and -B). The TgMYST-A genomic locus is singular and generates a approximately 3.5-kb transcript that can encode two proteins of 411 or 471 amino acids. TgMYST-B mRNA is approximately 7.0 kb and encodes a second MYST homologue. In addition to the canonical MYST HAT catalytic domain, both TgMYST-A and -B possess an atypical C2HC zinc finger and a chromodomain. Recombinant TgMYST-A exhibits a predilection to acetylate histone H4 in vitro at lysines 5, 8, 12, and 16. Antibody generated to TgMYST-A reveals that both the long and short (predominant) versions are present in the nucleus and are also plentiful in the cytoplasm. Moreover, both TgMYST-A forms are far more abundant in rapidly replicating parasites (tachyzoites) than encysted parasites (bradyzoites). A bioinformatics survey of the Toxoplasma genome reveals numerous homologues known to operate in native MYST complexes. The characterization of TgMYST HATs represents another important step toward understanding the regulation of gene expression in pathogenic protozoa and provides evolutionary insight into how these processes operate in eukaryotic cells in general.

Indexed as

5' Untranslated RegionsAmino Acid SequenceAnimalsAntibodies, ProtozoanBase SequenceCatalytic DomainCell LineCell NucleusCytoplasmGene Expression RegulationGenes, ProtozoanGenomeHistone AcetyltransferasesHumansLife Cycle StagesLysine5' Untranslated RegionsAntibodies, ProtozoanHistone AcetyltransferasesLysineProtozoan ProteinsRecombinant Proteins

Identifiers

PMID16339723
PMCPMC1317489
OpenAlexW2116840183

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.