Evidence map›Paper›PMID 10369665›Full record

ArticleThe EMBO journal1999

Protein tyrosine kinases in bacterial pathogens are associated with virulence and production of exopolysaccharide.

O Ilan, Y Bloch, G Frankel, H Ullrich, K Geider, I Rosenshine

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

53 citing papers in PubMed, 141 citations in OpenAlex.

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  10. The GTPase BipA expressed at low temperature inThe Journal of biological chemistry · 2018
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  13. Review
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  15. Article
  16. Mycobacterium tuberculosis supports protein tyrosine phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  17. Microbial protein-tyrosine kinases.The Journal of biological chemistry · 2014
    Review
  18. Article
  19. Article
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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

6 authors at 1 institution in 1 country.

O IlanDepartment of Molecular Genetics and Biotechnology, The Hebrew University Faculty of Medicine, PO Box 12272, Jerusalem 91120, Israel.
Y Bloch
G Frankel
H Ullrich
K Geider
I Rosenshine
Hebrew University of Jerusalem · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In eukaryotes, tyrosine protein phosphorylation has been studied extensively, while in bacteria, it is considered rare and is poorly defined. We demonstrate that Escherichia coli possesses a gene, etk, encoding an inner membrane protein that catalyses tyrosine autophosphorylation and phosphorylation of a synthetic co-polymer poly(Glu:Tyr). This protein tyrosine kinase (PTK) was termed Ep85 or Etk. All the E.coli strains examined possessed etk; however, only a subset of pathogenic strains expressed it. Etk is homologous to several bacterial proteins including the Ptk protein of Acinetobacter johnsonii, which is the only other known prokaryotic PTK. Other Etk homologues are AmsA of the plant pathogen Erwinia amylovora and Orf6 of the human pathogen Klebsiella pneumoniae. These proteins are involved in the production of exopolysaccharide (EPS) required for virulence. We demonstrated that like Etk, AmsA and probably also Orf6 are PTKs. Taken together, these findings suggest that tyrosine protein phosphorylation in prokaryotes is more common than was appreciated previously, and that Etk and its homologues define a distinct protein family of prokaryotic membrane-associated PTKs involved in EPS production and virulence. These prokaryotic PTKs may serve as a new target for the development of new antibiotics.

Indexed as

Escherichia coli ProteinsAmino Acid SequenceAntibodiesBacterial ProteinsCloning, MolecularCross ReactionsEnterobacteriaceaeEscherichia coliGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicIntracellular MembranesMembrane ProteinsMolecular Sequence DataOpen Reading FramesPhosphoproteinsPhosphorylationAntibodiesBacterial ProteinsBMX protein, humanEscherichia coli ProteinsEtk protein, E coliMembrane ProteinsPhosphoproteinsPhosphotyrosinePolysaccharides, BacterialProtein-Tyrosine Kinases

Identifiers

PMID10369665
PMCPMC1171405
OpenAlexW2119773053

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.