Evidence map›Paper›PMID 23852870›Full record

ArticleJournal of bacteriology2013

Acetylation of the response regulator RcsB controls transcription from a small RNA promoter.

Linda I Hu, Bui Khanh Chi, Misty L Kuhn, Ekaterina V Filippova, Arti J Walker-Peddakotla, Katrin Bäsell, Dörte Becher, Wayne F Anderson, Haike Antelmann, Alan J Wolfe

Abstract read
In one paragraph

Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
–field-weighted citation impact
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

66 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Sensory Systems and Transcriptional Regulation inFrontiers in bioengineering and biotechnology · 2022
    Review
  8. Article
  9. Review
  10. Contribution of NmSystems · 2021
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. The Rcs System inFrontiers in microbiology · 2021
    Review
  17. Review
  18. Article
  19. Article
  20. Article

6 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

10 authors.

Linda I HuDepartment of Microbiology and Immunology, Loyola University Chicago, Stritch School of Medicine, Maywood, IL, USA.
Bui Khanh Chi
Misty L Kuhn
Ekaterina V Filippova
Arti J Walker-Peddakotla
Katrin Bäsell
Dörte Becher
Wayne F Anderson
Haike Antelmann
Alan J Wolfe

Funding

Sensing central metabolic stressR01GM066130 · NIGMS · LOYOLA UNIVERSITY CHICAGO · PI WOLFE, ALAN J · 2004 to 2012
$2.7M
NIAID NIH HHS HHSN272200700058CNIAID NIH HHS HHSN272201200026CNIGMS NIH HHS GM066130NIGMS NIH HHS R01 GM066130
6 · The paper itself

Abstract

Nε-lysine acetylation was recently discovered on many bacterial proteins that function in diverse cellular processes. Thus, many questions remain unanswered. For example, what mechanisms regulate lysine acetylation? Does acetylation affect physiology? To help answer these questions, we studied the Escherichia coli response regulator and transcription factor RcsB, which is reported to be acetylated in vitro. To characterize RcsB acetylation, we monitored transcription from the rprA promoter, which requires RcsB. The conventional view is that RcsB is activated by phosphorylation through either the Rcs phosphorelay or acetyl phosphate. We affirmed that rprA transcription requires phosphorylated RcsB and showed that acetyl-phosphate (AcP) is a phosphoryl group donor to RcsB. However, a mutant that accumulates AcP (ackA) exhibited a reduction in rprA transcription instead of the predicted increase. rprA transcription also diminished in the cobB mutant, which lacks the only known E. coli protein deacetylase. This suggests the existence of an inhibitory mechanism that involves lysine acetylation, a supposition supported by the observation that RcsB isolated from the ackA or cobB mutant was hyperacetylated. Finally, we used a genetic approach to identify an AckA- and CobB-sensitive lysine (Lys-154) that controls RcsB activity. We propose that acetylation inhibits RcsB activity and that some of this inhibition acts through the acetylation of Lys-154.

Indexed as

AcetylationGene Expression Regulation, BacterialEscherichia coliEscherichia coli ProteinsLysinePhosphorylationPromoter Regions, GeneticRNATranscription FactorsEscherichia coli ProteinsLysineRcsB protein, E coliRNATranscription Factors

Identifiers

PMID23852870
PMCPMC3754749

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.