Evidence map›Paper›PMID 22544907›Full record

ArticleEukaryotic cell2012

Lysine acetylation is widespread on proteins of diverse function and localization in the protozoan parasite Toxoplasma gondii.

Victoria Jeffers, William J Sullivan

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
7.8field-weighted citation impact, top 1% 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

70 citing papers in PubMed, 116 citations in OpenAlex.

  1. Toxoplasma gondii SIR2A Promotes Tachyzoite Invasion via Lysine Deacetylase Activity.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  2. Review
  3. Article
  4. Host-Parasite Interactions inInternational journal of molecular sciences · 2024
    Article
  5. Article
  6. Proteomics Applications inPathogens (Basel, Switzerland) · 2023
    Review
  7. Article
  8. Article
  9. TgKDAC4: A Unique Deacetylase ofMicroorganisms · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

10 more citing papers are in PubMed but not listed here.

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

2 authors at 2 institutions in 1 country.

Victoria JeffersDepartment of Pharmacology and Toxicology, Indiana University School of Medicine, Indianapolis, Indiana, USA.
William J Sullivan
Indiana University – Purdue University Indianapolis · USIndiana University School of Medicine

Funding

GCN5-mediated transcription in AIDS pathogen ToxoplasmaR01AI077502 · NIAID · INDIANA UNIVERSITY INDIANAPOLIS · PI SULLIVAN, WILLIAM J · 2009 to 2013
$1.8M
MYST opportunities for Toxoplasma drug developmentR21AI083732 · NIAID · INDIANA UNIVERSITY INDIANAPOLIS · PI SULLIVAN, WILLIAM J · 2009 to 2010
$420k
GCN5-mediated transcription in AIDS pathogen ToxoplasmaR56AI077502 · NIAID · INDIANA UNIVERSITY INDIANAPOLIS · PI SULLIVAN, WILLIAM J · 2008 to 2008
$308k
NIAID NIH HHS AI077502NIAID NIH HHS AI083732NIAID NIH HHS R01 AI077502NIAID NIH HHS R21 AI083732NIAID NIH HHS R56 AI077502
6 · The paper itself

Abstract

While histone proteins are the founding members of lysine acetylation substrates, it is now clear that hundreds of other proteins can be acetylated in multiple compartments of the cell. Our knowledge of the scope of this modification throughout the kingdom of life is beginning to emerge, as proteome-wide lysine acetylation has been documented in prokaryotes, Arabidopsis thaliana, Drosophila melanogaster, and human cells. Using liquid chromatography-tandem mass spectrometry (LC-MS/MS) to identify parasite peptides enriched by immunopurification with acetyl-lysine antibody, we produced the first proteome-wide analysis of acetylation for a protozoan organism, the opportunistic apicomplexan parasite Toxoplasma gondii. The results show that lysine acetylation is abundant in the actively proliferating tachyzoite form of the parasite, which causes acute toxoplasmosis. Our approach successfully identified known acetylation marks on Toxoplasma histones and α-tubulin and detected over 400 novel acetylation sites on a wide variety of additional proteins, including those with roles in transcription, translation, metabolism, and stress responses. Importantly, an extensive set of parasite-specific proteins, including those found in organelles unique to Apicomplexa, is acetylated in the parasite. Our data provide a wealth of new information that improves our understanding of the evolution of this vital regulatory modification while potentially revealing novel therapeutic avenues. We conclude from this study that lysine acetylation was prevalent in the early stages of eukaryotic cell evolution and occurs on proteins involved in a remarkably diverse array of cellular functions, including those that are specific to parasites.

Indexed as

AcetylationAcetyltransferasesAmino Acid MotifsAmino Acid SequenceAnimalsChromatinCytoskeletonHistonesHumansLysineMolecular Sequence DataParasitesPeptidesProtein TransportProtozoan ProteinsToxoplasmaAcetyltransferasesChromatinHistonesLysinePeptidesProtozoan Proteins

Identifiers

PMID22544907
PMCPMC3370464
OpenAlexW2169147998

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.