Evidence map›Paper›PMID 24855643›Full record

ArticleThe Journal of biological chemistry2014

YfgM is an ancillary subunit of the SecYEG translocon in Escherichia coli.

Hansjörg Götzke, Isolde Palombo, Claudio Muheim, Elsa Perrody, Pierre Genevaux, Renuka Kudva, Matthias Müller, Daniel O Daley

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

34 citing papers in PubMed, 58 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. YidC fromBiomolecules · 2023
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021
    Review
  15. A Novel GeneFrontiers in microbiology · 2021
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

8 authors at 4 institutions in 3 countries.

Hansjörg GötzkeFrom the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.
Isolde PalomboFrom the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.
Claudio MuheimFrom the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.
Elsa PerrodyLaboratoire de Microbiologie et Génétique Moléculaires, CNRS, and Université Paul Sabatier, 31062 Toulouse, France, and.
Pierre GenevauxLaboratoire de Microbiologie et Génétique Moléculaires, CNRS, and Université Paul Sabatier, 31062 Toulouse, France, and.
Renuka KudvaInstitute of Biochemistry and Molecular Biology, Zentrum für Biochemie und Molekulare, Spemann Graduate School of Biology and Medicine, University of Freiburg, D-79104 Freiburg, Germany.
Matthias MüllerInstitute of Biochemistry and Molecular Biology, Zentrum für Biochemie und Molekulare, Spemann Graduate School of Biology and Medicine, University of Freiburg, D-79104 Freiburg, Germany.
Daniel O DaleyFrom the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden, ddaley@dbb.su.se.
Stockholm University · SEUniversity of Freiburg · DECentre National de la Recherche Scientifique · FRUniversité Toulouse III - Paul Sabatier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein secretion in Gram-negative bacteria is essential for both cell viability and pathogenesis. The vast majority of secreted proteins exit the cytoplasm through a transmembrane conduit called the Sec translocon in a process that is facilitated by ancillary modules, such as SecA, SecDF-YajC, YidC, and PpiD. In this study we have characterized YfgM, a protein with no annotated function. We found it to be a novel ancillary subunit of the Sec translocon as it co-purifies with both PpiD and the SecYEG translocon after immunoprecipitation and blue native/SDS-PAGE. Phenotypic analyses of strains lacking yfgM suggest that its physiological role in the cell overlaps with the periplasmic chaperones SurA and Skp. We, therefore, propose a role for YfgM in mediating the trafficking of proteins from the Sec translocon to the periplasmic chaperone network that contains SurA, Skp, DegP, PpiD, and FkpA.

Indexed as

Cell MembraneDNA-Binding ProteinsEscherichia coliEscherichia coli ProteinsGene DeletionMolecular ChaperonesOxidative StressPeriplasmProtein SubunitsProtein TransportSEC Translocation ChannelsDNA-Binding ProteinsEscherichia coli ProteinsMolecular ChaperonesProtein SubunitsSEC Translocation ChannelsSkp protein, E coliYfgM protein, E coliBN-PAGEEscherichia coli (E. coli)Membrane BiogenesisMembrane ProteinPeriplasmic ChaperonesProtein SecretionProtein TranslocationSecYEG Translocon

Identifiers

PMID24855643
PMCPMC4081946
OpenAlexW2007111091

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.