Evidence map›Paper›PMID 21217812›Full record

ArticlePloS one2010

Nε-lysine acetylation of a bacterial transcription factor inhibits Its DNA-binding activity.

Sandy Thao, Chien-Sheng Chen, Heng Zhu, Jorge C Escalante-Semerena

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed
8.3field-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

97 citing papers in PubMed, 143 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Insights into the Lysine Acetylome of the HaloarchaeonAntioxidants (Basel, Switzerland) · 2023
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  11. Article
  12. Contribution of NmSystems · 2021
    Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Review
  19. The Phage-EncodedViruses · 2020
    Article
  20. Article

37 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

4 authors at 2 institutions in 2 countries.

Sandy ThaoDepartment of Bacteriology, University of Wisconsin, Madison, Wisconsin, United States of America.
Chien-Sheng Chen
Heng Zhu
Jorge C Escalante-Semerena
Johns Hopkins University · USUniversity of Wisconsin–Madison · US

Funding

TCP5: ACTIVE SITE LABELING REAGENT FOR ACETYLTRANSFERASESU54RR020839 · NCRR · JOHNS HOPKINS UNIVERSITY · PI BOEKE, JEF D · 2004 to 2011
$27.4M
Sirtuins and Metabolic Pathway IntegrationR01GM062203 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI ESCALANTE, JORGE C · 2001 to 2017
$4.7M
Studies of a Bacterial Protein N-Lysine AcetyltransferaseF31GM083668 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI THAO, SANDY · 2008 to 2010
$55k
NCRR NIH HHS U54 RR 020839NCRR NIH HHS U54 RR020839NIGMS NIH HHS F31 GM083668NIGMS NIH HHS F31-GM083668NIGMS NIH HHS R01 GM062203NIGMS NIH HHS R01-GM62203
6 · The paper itself

Abstract

Evidence suggesting that eukaryotes and archaea use reversible N(ε)-lysine (N(ε)-Lys) acetylation to modulate gene expression has been reported, but evidence for bacterial use of N(ε)-Lys acetylation for this purpose is lacking. Here, we report data in support of the notion that bacteria can control gene expression by modulating the acetylation state of transcription factors (TFs). We screened the E. coli proteome for substrates of the bacterial Gcn5-like protein acetyltransferase (Pat). Pat acetylated four TFs, including the RcsB global regulatory protein, which controls cell division, and capsule and flagellum biosynthesis in many bacteria. Pat acetylated residue Lys180 of RcsB, and the NAD(+)-dependent Sir2 (sirtuin)-like protein deacetylase (CobB) deacetylated acetylated RcsB (RcsB(Ac)), demonstrating that N(ε)-Lys acetylation of RcsB is reversible. Analysis of RcsB(Ac) and variant RcsB proteins carrying substitutions at Lys180 provided biochemical and physiological evidence implicating Lys180 as a critical residue for RcsB DNA-binding activity. These findings further the likelihood that reversible N(ε)-Lys acetylation of transcription factors is a mode of regulation of gene expression used by all cells.

Indexed as

Gene Expression Regulation, BacterialAcetylationAcetyltransferasesBacteriaCell DivisionDNAEscherichia coliEscherichia coli ProteinsFlagellaLysinePlasmidsProtein Array AnalysisProtein BindingProteomeProteomicsSirtuinsAcetyltransferasescobB protein, E ColiDNAEscherichia coli ProteinsLysineprotein N-terminal acetyltransferaseProteomeSirtuins

Identifiers

PMID21217812
PMCPMC3013089
OpenAlexW2094685393

What OpenQuestion 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 OpenQuestion graph.