Evidence map›Paper›PMID 35217658›Full record

ArticleNature communications2022

Inhibition of SRP-dependent protein secretion by the bacterial alarmone (p)ppGpp.

Laura Czech, Christopher-Nils Mais, Hanna Kratzat, Pinku Sarmah, Pietro Giammarinaro, Sven-Andreas Freibert, Hanna Folke Esser, Joanna Musial, Otto Berninghausen, Wieland Steinchen and 3 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
7.1field-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

24 citing papers in PubMed, 41 citations in OpenAlex.

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  12. (p)ppGpp mediates persister formation inFrontiers in microbiology · 2025
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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

13 authors at 4 institutions in 1 country.

Laura Czech *Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry Philipps-Universität Marburg, Marburg, Germany. laura.czech@staff.uni-marburg.de.ORCID http://orcid.org/0000-0001-7398-1186
Christopher-Nils Mais *Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry Philipps-Universität Marburg, Marburg, Germany.ORCID http://orcid.org/0000-0003-1927-2885
Hanna KratzatGene Center Munich, Department of Biochemistry, Ludwig-Maximilians-Universität, LMU, Munich, Germany.ORCID http://orcid.org/0000-0001-5849-6131
Pinku SarmahInstitute of Biochemistry and Molecular Biology, Faculty of Medicine, Albert-Ludwigs-Universität Freiburg, Freiburg, Germany.
Pietro GiammarinaroCenter for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry Philipps-Universität Marburg, Marburg, Germany.
Sven-Andreas FreibertInstitut für Zytobiologie, Philipps-Universität Marburg, Marburg, Germany.ORCID http://orcid.org/0000-0002-8521-2963
Hanna Folke EsserGene Center Munich, Department of Biochemistry, Ludwig-Maximilians-Universität, LMU, Munich, Germany.
Joanna MusialGene Center Munich, Department of Biochemistry, Ludwig-Maximilians-Universität, LMU, Munich, Germany.
Otto BerninghausenGene Center Munich, Department of Biochemistry, Ludwig-Maximilians-Universität, LMU, Munich, Germany.ORCID http://orcid.org/0000-0002-9255-0522
Wieland SteinchenCenter for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry Philipps-Universität Marburg, Marburg, Germany.
Roland BeckmannGene Center Munich, Department of Biochemistry, Ludwig-Maximilians-Universität, LMU, Munich, Germany.ORCID http://orcid.org/0000-0003-4291-3898
Hans-Georg KochInstitute of Biochemistry and Molecular Biology, Faculty of Medicine, Albert-Ludwigs-Universität Freiburg, Freiburg, Germany.ORCID http://orcid.org/0000-0001-5913-0334
Gert BangeCenter for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry Philipps-Universität Marburg, Marburg, Germany. gert.bange@synmikro.uni-marburg.de.ORCID http://orcid.org/0000-0002-7826-0932
Ludwig-Maximilians-Universität München · DEPhilipps University of Marburg · DEUniversity of Freiburg · DELoewe Center for Synthetic Microbiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The stringent response enables bacteria to respond to nutrient limitation and other stress conditions through production of the nucleotide-based second messengers ppGpp and pppGpp, collectively known as (p)ppGpp. Here, we report that (p)ppGpp inhibits the signal recognition particle (SRP)-dependent protein targeting pathway, which is essential for membrane protein biogenesis and protein secretion. More specifically, (p)ppGpp binds to the SRP GTPases Ffh and FtsY, and inhibits the formation of the SRP receptor-targeting complex, which is central for the coordinated binding of the translating ribosome to the SecYEG translocon. Cryo-EM analysis of SRP bound to translating ribosomes suggests that (p)ppGpp may induce a distinct conformational stabilization of the NG domain of Ffh and FtsY in Bacillus subtilis but not in E. coli.

Indexed as

Escherichia coli ProteinsSignal Recognition ParticleBacterial ProteinsEscherichia coliGuanosine PentaphosphateProtein BindingReceptors, Cytoplasmic and NuclearBacterial ProteinsEscherichia coli ProteinsGuanosine PentaphosphateReceptors, Cytoplasmic and NuclearSignal Recognition Particle

Identifiers

PMID35217658
PMCPMC8881573
OpenAlexW4214638688

What OpenQuestion holds

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LicenceCC BY
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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.