Evidence map›Paper›PMID 26092727›Full record

ArticleThe Journal of biological chemistry2015

Conditional Proteolysis of the Membrane Protein YfgM by the FtsH Protease Depends on a Novel N-terminal Degron.

Lisa-Marie Bittner, Kai Westphal, Franz Narberhaus

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

22 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. RcsF-independent mechanisms of signaling within the Rcs Phosphorelay.bioRxiv : the preprint server for biology · 2024
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  7. Suppressors ofInternational journal of molecular sciences · 2023
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  8. Review
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  10. Frontiers in microbiology · 2021
    Article
  11. The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Multifunctional Mitochondrial AAA Proteases.Frontiers in molecular biosciences · 2017
    Review
  19. Review
  20. 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

3 authors at 1 institution in 1 country.

Lisa-Marie BittnerFrom Microbial Biology, Ruhr University Bochum, 44801 Bochum, Germany.
Kai WestphalFrom Microbial Biology, Ruhr University Bochum, 44801 Bochum, Germany.
Franz NarberhausFrom Microbial Biology, Ruhr University Bochum, 44801 Bochum, Germany franz.narberhaus@rub.de.
Ruhr University Bochum · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Regulated proteolysis efficiently and rapidly adapts the bacterial proteome to changing environmental conditions. Many protease substrates contain recognition motifs, so-called degrons, that direct them to the appropriate protease. Here we describe an entirely new degron identified in the cytoplasmic N-terminal end of the membrane-anchored protein YfgM of Escherichia coli. YfgM is stable during exponential growth and degraded in stationary phase by the essential FtsH protease. The alarmone (p)ppGpp, but not the previously described YfgM interactors RcsB and PpiD, influence YfgM degradation. By scanning mutagenesis, we define individual amino acids responsible for turnover of YfgM and find that the degron does not at all comply with the known N-end rule pathway. The YfgM degron is a distinct module that facilitates FtsH-mediated degradation when fused to the N terminus of another monotopic membrane protein but not to that of a cytoplasmic protein. Several lines of evidence suggest that stress-induced degradation of YfgM relieves the response regulator RcsB and thereby permits cellular protection by the Rcs phosphorelay system. On the basis of these and other results in the literature, we propose a model for how the membrane-spanning YfgM protein serves as connector between the stress responses in the periplasm and cytoplasm.

Indexed as

Amino Acid SequenceATP-Dependent ProteasesEscherichia coli ProteinsMolecular ChaperonesMolecular Sequence DataPeptidylprolyl IsomeraseProtein StabilityProteolysisStress, PhysiologicalTranscription FactorsATP-Dependent ProteasesEscherichia coli ProteinsFtsH protein, E coliMolecular ChaperonesPeptidylprolyl IsomerasePpiD protein, E coliRcsB protein, E coliTranscription FactorsYfgM protein, E coliATP-dependent proteaseEscherichia coli (E. coli)proteaseprotein degradationRcs phosphorelay systemstress response

Identifiers

PMID26092727
PMCPMC4521054
OpenAlexW2225358282

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.