Evidence map›Paper›PMID 23234799›Full record

ArticleJournal of proteomics2013

Differential lysine acetylation profiles of Erwinia amylovora strains revealed by proteomics.

Xia Wu, Adaikkalam Vellaichamy, Dongping Wang, Leonid Zamdborg, Neil L Kelleher, Steven C Huber, Youfu Zhao

Abstract read
In one paragraph

Article in Journal of proteomics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
10.5field-weighted citation impact, top 2% 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

40 citing papers in PubMed, 84 citations in OpenAlex.

  1. NProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. YkuR functions as a protein deacetylase inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Bacterial protein acetylation: mechanisms, functions, and methods for study.Frontiers in cellular and infection microbiology · 2024
    Review
  4. Article
  5. Article
  6. Review
  7. The Phage-EncodedViruses · 2020
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Identification of Acetylated Proteins in Borrelia burgdorferi.Methods in molecular biology (Clifton, N.J.) · 2018
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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 4 institutions in 1 country.

Xia WuDepartment of Plant Biology, University of Illinois, Urbana, IL 61801, USA.
Adaikkalam Vellaichamy
Dongping Wang
Leonid Zamdborg
Neil L Kelleher
Steven C Huber
Youfu Zhao
University of Illinois Urbana-Champaign · USMethodist Hospital · USNorthwestern University · USUrbana University · US

Funding

Deciphering the Histone Code by Mass Spectrometry and High Dimensional StatisticsF30DA026672 · NIDA · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI ZAMDBORG, LEONID · 2010 to 2012
$140k
NIDA NIH HHS 1F30DA026672NIDA NIH HHS F30 DA026672
6 · The paper itself

Abstract

Protein lysine acetylation (LysAc) has recently been demonstrated to be widespread in E. coli and Salmonella, and to broadly regulate bacterial physiology and metabolism. However, LysAc in plant pathogenic bacteria is largely unknown. Here we first report the lysine acetylome of Erwinia amylovora, an enterobacterium causing serious fire blight disease of apples and pears. Immunoblots using generic anti-lysine acetylation antibodies demonstrated that growth conditions strongly affected the LysAc profiles in E. amylovora. Differential LysAc profiles were also observed for two E. amylovora strains, known to have differential virulence in plants, indicating translational modification of proteins may be important in determining virulence of bacterial strains. Proteomic analysis of LysAc in two E. amylovora strains identified 141 LysAc sites in 96 proteins that function in a wide range of biological pathways. Consistent with previous reports, 44% of the proteins are involved in metabolic processes, including central metabolism, lipopolysaccharide, nucleotide and amino acid metabolism. Interestingly, for the first time, several proteins involved in E. amylovora virulence, including exopolysaccharide amylovoran biosynthesis- and type III secretion-associated proteins, were found to be lysine acetylated, suggesting that LysAc may play a major role in bacterial virulence. Comparative analysis of LysAc sites in E. amylovora and E. coli further revealed the sequence and structural commonality for LysAc in the two organisms. Collectively, these results reinforce the notion that LysAc of proteins is widespread in bacterial metabolism and virulence.

Indexed as

AcetylationBacterial ProteinsChromatography, LiquidErwinia amylovoraLysinePlant DiseasesProtein Processing, Post-TranslationalProteomicsTandem Mass SpectrometryVirulenceBacterial ProteinsLysine

Identifiers

PMID23234799
PMCPMC4418653
OpenAlexW2045071318

What OpenQuestion holds

Textmetadata
LicenceTDM
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.