Evidence map›Paper›PMID 36537800›Full record

ArticlemSystems2023

E. coli Toxin YjjJ (HipH) Is a Ser/Thr Protein Kinase That Impacts Cell Division, Carbon Metabolism, and Ribosome Assembly.

Fabio Lino Gratani, Till Englert, Payal Nashier, Peter Sass, Laura Czech, Niels Neumann, Sofia Doello, Petra Mann, Rudolf Blobelt, Siegfried Alberti and 4 more

Open access · goldAbstract read
In one paragraph

Article in mSystems, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

8 citing papers in PubMed, 14 citations in OpenAlex.

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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

14 authors at 3 institutions in 1 country.

Fabio Lino GrataniQuantitative Proteomics, Interfaculty Institute of Cell Biology, University of Tübingen, Tübingen, Germany.
Till EnglertQuantitative Proteomics, Interfaculty Institute of Cell Biology, University of Tübingen, Tübingen, Germany.
Payal NashierQuantitative Proteomics, Interfaculty Institute of Cell Biology, University of Tübingen, Tübingen, Germany.
Peter SassMicrobial Bioactive Compounds, Interfaculty Institute for Microbiology and Infection Medicine, University of Tübingen, Tübingen, Germany.ORCID 0000-0002-4477-2382
Laura CzechSYNMIKRO Research Center & Faculty of Chemistry, University of Marburg, Marburg, Germany.
Niels NeumannOrganismic Interactions, Interfaculty Institute for Microbiology and Infection Medicine, University of Tübingen, Tübingen, Germany.
Sofia DoelloOrganismic Interactions, Interfaculty Institute for Microbiology and Infection Medicine, University of Tübingen, Tübingen, Germany.ORCID 0000-0002-4025-3016
Petra MannMax Planck Institute for Terrestrial Microbiology, Marburg, Germany.
Rudolf BlobeltQuantitative Proteomics, Interfaculty Institute of Cell Biology, University of Tübingen, Tübingen, Germany.
Siegfried AlbertiQuantitative Proteomics, Interfaculty Institute of Cell Biology, University of Tübingen, Tübingen, Germany.
Karl ForchhammerOrganismic Interactions, Interfaculty Institute for Microbiology and Infection Medicine, University of Tübingen, Tübingen, Germany.ORCID 0000-0003-3199-8101
Gert BangeSYNMIKRO Research Center & Faculty of Chemistry, University of Marburg, Marburg, Germany.ORCID 0000-0002-7826-0932
Katharina HöferMax Planck Institute for Terrestrial Microbiology, Marburg, Germany.
Boris MacekQuantitative Proteomics, Interfaculty Institute of Cell Biology, University of Tübingen, Tübingen, Germany.
University of Tübingen · DELoewe Center for Synthetic Microbiology · DEMax Planck Institute for Terrestrial Microbiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein Ser/Thr kinases are posttranslational regulators of key molecular processes in bacteria, such as cell division and antibiotic tolerance. Here, we characterize the E. coli toxin YjjJ (HipH), a putative protein kinase annotated as a member of the family of HipA-like Ser/Thr kinases, which are involved in antibiotic tolerance. Using SILAC-based phosphoproteomics we provide experimental evidence that YjjJ is a Ser/Thr protein kinase and its primary protein substrates are the ribosomal protein RpmE (L31) and the carbon storage regulator CsrA. YjjJ activity impacts ribosome assembly, cell division, and central carbon metabolism but it does not increase antibiotic tolerance as does its homologue HipA. Intriguingly, overproduction of YjjJ and its kinase-deficient variant can activate HipA and other kinases, pointing to a cross talk between Ser/Thr kinases in E. coli.

Indexed as

Escherichia coliEscherichia coli ProteinsProtein Serine-Threonine KinasesAnti-Bacterial AgentsBacteriaBacterial ToxinsCell DivisionEnterotoxinsRepressor ProteinsRibosomal ProteinsRibosomesRNA-Binding ProteinsAnti-Bacterial AgentsBacterial ToxinsCsrA protein, E coliEnterotoxinsEscherichia coli ProteinshipA protein, E coliProtein Serine-Threonine KinasesRepressor ProteinsRibosomal ProteinsRNA-Binding ProteinsYjjJ protein, E colicell divisionkinasesmetabolismphosphoproteomicsproteomicsserine/threonine kinases

Identifiers

PMID36537800
PMCPMC9948734
OpenAlexW4312019906

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.