Evidence map›Paper›PMID 28398568›Full record

ArticleNucleic acids research2017

Deacetylation of topoisomerase I is an important physiological function of E. coli CobB.

Qingxuan Zhou, Yan Ning Zhou, Ding Jun Jin, Yuk-Ching Tse-Dinh

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

23 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. YkuR functions as a protein deacetylase inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Article
  8. Review
  9. Insights into the Lysine Acetylome of the HaloarchaeonAntioxidants (Basel, Switzerland) · 2023
    Article
  10. Article
  11. Mechanism of Type IA Topoisomerases.Molecules (Basel, Switzerland) · 2020
    Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Protein Acetylation in Bacteria.Annual review of microbiology · 2019
    Review
  17. Article
  18. Review
  19. Review
  20. Biochemical Basis ofInternational journal of molecular sciences · 2018
    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

4 authors at 3 institutions in 1 country.

Qingxuan ZhouDepartment of Chemistry and Biochemistry, Florida International University, Miami, FL 33199, USA.
Yan Ning ZhouTranscription Control Section, RNA Biology Laboratory, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, USA.
Ding Jun JinTranscription Control Section, RNA Biology Laboratory, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, USA.
Yuk-Ching Tse-DinhDepartment of Chemistry and Biochemistry, Florida International University, Miami, FL 33199, USA.
Florida International University · USNational Cancer Institute · USNational Institutes of Health · US

Funding

Transcription Regulation in E. coli and H. pyloriZIABC010632 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI JIN, DING JUN · 2009 to 2019
$11.9M
Supplement for undergraduate research participant to promote diversityR01GM054226 · NIGMS · NEW YORK MEDICAL COLLEGE · PI TSE-DINH, YUK-CHING · 1996 to 2020
$4.6M
NIGMS NIH HHS R01 GM054226
6 · The paper itself

Abstract

Escherichia coli topoisomerase I (TopA), a regulator of global and local DNA supercoiling, is modified by Nε-Lysine acetylation. The NAD+-dependent protein deacetylase CobB can reverse both enzymatic and non-enzymatic lysine acetylation modification in E. coli. Here, we show that the absence of CobB in a ΔcobB mutant reduces intracellular TopA catalytic activity and increases negative DNA supercoiling. TopA expression level is elevated as topA transcription responds to the increased negative supercoiling. The slow growth phenotype of the ΔcobB mutant can be partially compensated by further increase of intracellular TopA level via overexpression of recombinant TopA. The relaxation activity of purified TopA is decreased by in vitro non-enzymatic acetyl phosphate mediated lysine acetylation, and the presence of purified CobB protects TopA from inactivation by such non-enzymatic acetylation. The specific activity of TopA expressed from His-tagged fusion construct in the chromosome is inversely proportional to the degree of in vivo lysine acetylation during growth transition and growth arrest. These findings demonstrate that E. coli TopA catalytic activity can be modulated by lysine acetylation-deacetylation, and prevention of TopA inactivation from excess lysine acetylation and consequent increase in negative DNA supercoiling is an important physiological function of the CobB protein deacetylase.

Indexed as

AcetylationBiocatalysisChromosomes, BacterialDNA, BacterialDNA, SuperhelicalDNA Topoisomerases, Type IElectrophoresis, Agar GelEscherichia coliEscherichia coli ProteinsLysineMutationPhenotypeProtein BindingProteomicsRecombinant ProteinsSirtuinscobB protein, E ColiDNA, BacterialDNA, SuperhelicalDNA Topoisomerases, Type IEscherichia coli ProteinsLysineRecombinant ProteinsSirtuins

Identifiers

PMID28398568
PMCPMC5605244
OpenAlexW2604753901

What OpenQuestion holds

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LicenceCC BY-NC
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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.