Evidence map›Paper›PMID 23355473›Full record

ArticleThe Journal of biological chemistry2013

Charge composition features of model single-span membrane proteins that determine selection of YidC and SecYEG translocase pathways in Escherichia coli.

Lu Zhu, Abdul Wasey, Stephen H White, Ross E Dalbey

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.8field-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

17 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. The versatile role of YidC in membrane protein biosynthesis and quality control.Biochimica et biophysica acta. Molecular cell research · 2025
    Review
  3. Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. YidC/Alb3/Oxa1 Family of Insertases.The Journal of biological chemistry · 2015
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. 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

4 authors at 2 institutions in 1 country.

Lu ZhuDepartment of Chemistry and Biochemistry, Ohio State University, Columbus, Ohio 43210.
Abdul WaseyDepartment of Chemistry and Biochemistry, Ohio State University, Columbus, Ohio 43210.
Stephen H WhiteDepartment of Physiology and Biophysics, University of California, Irvine, California 92697-4560.
Ross E DalbeyDepartment of Chemistry and Biochemistry, Ohio State University, Columbus, Ohio 43210. Electronic address: dalbey@chemistry.ohio-state.edu.
The Ohio State University · USUniversity of California, Irvine · US

Funding

Membrane Protein Folding and AssemblyR01GM074637 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI WHITE, STEPHEN H. · 2006 to 2020
$4.5M
NIGMS NIH HHS GM074637NIGMS NIH HHS R01 GM074637
6 · The paper itself

Abstract

We have investigated the features of single-span model membrane proteins based upon leader peptidase that determines whether the proteins insert by a YidC/Sec-independent, YidC-only, or YidC/Sec mechanism. We find that a protein with a highly hydrophobic transmembrane segment that inserts into the membrane by a YidC/Sec-independent mechanism becomes YidC-dependent if negatively charged residues are inserted into the translocated periplasmic domain or if the hydrophobicity of the transmembrane segment is reduced by substituting polar residues for nonpolar ones. This suggests that charged residues in the translocated domain and the hydrophobicity within the transmembrane segment are important determinants of the insertion pathway. Strikingly, the addition of a positively charged residue to either the translocated region or the transmembrane region can switch the insertion requirements such that insertion requires both YidC and SecYEG. To test conclusions from the model protein studies, we confirmed that a positively charged residue is a SecYEG determinant for the endogenous proteins ATP synthase subunits a and b and the TatC subunit of the Tat translocase. These findings provide deeper insights into how pathways are selected for the insertion of proteins into the Escherichia coli inner membrane.

Indexed as

Gene Expression Regulation, BacterialAmino Acid SequenceBiophysicsEscherichia coliEscherichia coli ProteinsMembrane Transport ProteinsModels, BiologicalMolecular Sequence DataMutagenesis, Site-DirectedPlasmidsProtein ConformationProtein Structure, TertiaryProtein TransportProton-Motive ForceSEC Translocation ChannelsThermodynamicsEscherichia coli ProteinsMembrane Transport ProteinsSEC Translocation ChannelsYIDC protein, E coli

Identifiers

PMID23355473
PMCPMC3597811
OpenAlexW2167154159

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.