Evidence map›Paper›PMID 27924919›Full record

ArticleScientific reports2016

A central cavity within the holo-translocon suggests a mechanism for membrane protein insertion.

Mathieu Botte, Nathan R Zaccai, Jelger Lycklama À Nijeholt, Remy Martin, Kèvin Knoops, Gabor Papai, Juan Zou, Aurélien Deniaud, Manikandan Karuppasamy, Qiyang Jiang and 8 more

Abstract read
In one paragraph

Article in Scientific reports, 2016. 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
–field-weighted citation impact
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.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. The versatile role of YidC in membrane protein biosynthesis and quality control.Biochimica et biophysica acta. Molecular cell research · 2025
    Review
  7. Article
  8. Article
  9. The Biogenesis of Multipass Membrane Proteins.Cold Spring Harbor perspectives in biology · 2023
    Review
  10. Article
  11. Article
  12. The mechanisms of integral membrane protein biogenesis.Nature reviews. Molecular cell biology · 2022
    Review
  13. Review
  14. Cotranslational Biogenesis of Membrane Proteins in Bacteria.Frontiers in molecular biosciences · 2022
    Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review
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

18 authors.

Mathieu BotteEuropean Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, 38042 Grenoble, France.
Nathan R ZaccaiSchool of Biochemistry, University of Bristol, BS8 1TD, United Kingdom.
Jelger Lycklama À NijeholtEuropean Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, 38042 Grenoble, France.
Remy MartinSchool of Biochemistry, University of Bristol, BS8 1TD, United Kingdom.
Kèvin KnoopsEuropean Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, 38042 Grenoble, France.
Gabor PapaiDepartment of Integrated Structural Biology, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), U964 INSERM, UMR7104 CNRS; University of Strasbourg, 1 Rue Laurent Fries, BP10142, 67404 Illkirch, France.
Juan ZouWellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh, EH9 3JR, United Kingdom.
Aurélien DeniaudEuropean Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, 38042 Grenoble, France.
Manikandan KaruppasamyEuropean Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, 38042 Grenoble, France.
Qiyang JiangEuropean Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, 38042 Grenoble, France.
Abhishek Singha RoyDepartment of Physics, University of Illinois Urbana Champaign, 3217 Beckman Institute, 405 N Mathews Ave., Urbana, IL 61801, USA.
Klaus SchultenDepartment of Physics, University of Illinois Urbana Champaign, 3217 Beckman Institute, 405 N Mathews Ave., Urbana, IL 61801, USA.
Patrick SchultzDepartment of Integrated Structural Biology, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), U964 INSERM, UMR7104 CNRS; University of Strasbourg, 1 Rue Laurent Fries, BP10142, 67404 Illkirch, France.
Juri RappsilberWellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh, EH9 3JR, United Kingdom.
Giuseppe ZaccaiInstitut Laue Langevin, 71 Avenue des Martyrs, F-38042 Grenoble, France.
Imre BergerEuropean Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, 38042 Grenoble, France.
Ian CollinsonSchool of Biochemistry, University of Bristol, BS8 1TD, United Kingdom.
Christiane SchaffitzelEuropean Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, 38042 Grenoble, France.

Funding

Biotechnology and Biological Sciences Research Council BB/I008675/1Biotechnology and Biological Sciences Research Council BB/M003604/1Biotechnology and Biological Sciences Research Council BB/P000940/1Wellcome Trust 092076Wellcome Trust 103139Wellcome Trust 103139/Z/13/ZWellcome Trust 108504
6 · The paper itself

Abstract

The conserved SecYEG protein-conducting channel and the accessory proteins SecDF-YajC and YidC constitute the bacterial holo-translocon (HTL), capable of protein-secretion and membrane-protein insertion. By employing an integrative approach combining small-angle neutron scattering (SANS), low-resolution electron microscopy and biophysical analyses we determined the arrangement of the proteins and lipids within the super-complex. The results guided the placement of X-ray structures of individual HTL components and allowed the proposal of a model of the functional translocon. Their arrangement around a central lipid-containing pool conveys an unexpected, but compelling mechanism for membrane-protein insertion. The periplasmic domains of YidC and SecD are poised at the protein-channel exit-site of SecY, presumably to aid the emergence of translocating polypeptides. The SecY lateral gate for membrane-insertion is adjacent to the membrane 'insertase' YidC. Absolute-scale SANS employing a novel contrast-match-point analysis revealed a dynamic complex adopting open and compact configurations around an adaptable central lipid-filled chamber, wherein polytopic membrane-proteins could fold, sheltered from aggregation and proteolysis.

Indexed as

Binding SitesCloning, MolecularCryoelectron MicroscopyEscherichia coliEscherichia coli ProteinsGene ExpressionGenetic VectorsMembrane Transport ProteinsMethanocaldococcusModels, MolecularNeutron DiffractionProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsProtein TransportEscherichia coli ProteinsMembrane Transport ProteinsRecombinant ProteinsSecD protein, E coliSEC Translocation ChannelsSecY protein, E coliYIDC protein, E coli

Identifiers

PMID27924919
PMCPMC5141469

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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.