Evidence map›Paper›PMID 22373819›Full record

ArticleMolecular systems biology2012

Cross-talk between phosphorylation and lysine acetylation in a genome-reduced bacterium.

Vera van Noort, Jan Seebacher, Samuel Bader, Shabaz Mohammed, Ivana Vonkova, Matthew J Betts, Sebastian Kühner, Runjun Kumar, Tobias Maier, Martina O'Flaherty and 9 more

Open access · goldAbstract read
In one paragraph

Article in Molecular systems biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed
12.6field-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

88 citing papers in PubMed, 176 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Unveiling the stealthy tactics: mycoplasma's immune evasion strategies.Frontiers in cellular and infection microbiology · 2023
    Review
  9. Article
  10. Article
  11. Frontiers in microbiology · 2022
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Acetylation of Response Regulator Protein MtrA inFrontiers in microbiology · 2020
    Article
  20. Review

28 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

19 authors at 6 institutions in 3 countries.

Vera van NoortStructural and Computational Biology Unit, European Molecular Biology Laboratory, EMBL, Heidelberg, Germany.
Jan Seebacher
Samuel Bader
Shabaz Mohammed
Ivana Vonkova
Matthew J Betts
Sebastian Kühner
Runjun Kumar
Tobias Maier
Martina O'Flaherty
Vladimir Rybin
Arne Schmeisky
Eva Yus
Jörg Stülke
Luis Serrano
Robert B Russell
Albert J R Heck
Peer Bork
Anne-Claude Gavin
European Molecular Biology Laboratory · DEUtrecht University · NLCentre for Genomic Regulation · ESHeidelberg University · DEUniversity of Göttingen · DEInstitució Catalana de Recerca i Estudis Avançats · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein post-translational modifications (PTMs) represent important regulatory states that when combined have been hypothesized to act as molecular codes and to generate a functional diversity beyond genome and transcriptome. We systematically investigate the interplay of protein phosphorylation with other post-transcriptional regulatory mechanisms in the genome-reduced bacterium Mycoplasma pneumoniae. Systematic perturbations by deletion of its only two protein kinases and its unique protein phosphatase identified not only the protein-specific effect on the phosphorylation network, but also a modulation of proteome abundance and lysine acetylation patterns, mostly in the absence of transcriptional changes. Reciprocally, deletion of the two putative N-acetyltransferases affects protein phosphorylation, confirming cross-talk between the two PTMs. The measured M. pneumoniae phosphoproteome and lysine acetylome revealed that both PTMs are very common, that (as in Eukaryotes) they often co-occur within the same protein and that they are frequently observed at interaction interfaces and in multifunctional proteins. The results imply previously unreported hidden layers of post-transcriptional regulation intertwining phosphorylation with lysine acetylation and other mechanisms that define the functional state of a cell.

Indexed as

AcetylationAcetylesteraseCatalytic DomainEvolution, MolecularGene Regulatory NetworksGenome, BacterialGenome SizeLysineMetabolic Networks and PathwaysModels, BiologicalOrganisms, Genetically ModifiedPhosphorylationPneumonia, MycoplasmaProtein KinasesProtein Processing, Post-TranslationalProteomeAcetylesteraseLysineProtein KinasesProteome

Identifiers

PMID22373819
PMCPMC3293634
OpenAlexW2111896563

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.