Evidence map›Paper›PMID 7556084›Full record

ArticleThe EMBO journal1995

A new genetic selection identifies essential residues in SecG, a component of the Escherichia coli protein export machinery.

S Bost, D Belin

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.9field-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

18 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. The bacterial Sec-translocase: structure and mechanism.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012
    Review
  7. Article
  8. Topologically fixed SecG is fully functional.Journal of bacteriology · 2006
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Roles of SecG in ATP- and SecA-dependent protein translocation.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
  16. Linkage map of Escherichia coli K-12, edition 10: the traditional map.Microbiology and molecular biology reviews : MMBR · 1998
    Review
  17. Article
  18. 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

2 authors at 1 institution in 1 country.

S BostDépartment de Pathologie, Université de Genève, Switzerland.
D Belin
University of Geneva · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The signal sequence of the murine serine protease inhibitor PAI-2 promotes alkaline phosphatase export to the E. coli periplasm. However, high level expression of this chimeric protein interferes with cell growth. Since most suppressors of this toxic phenotype map to secA and secY, growth arrest results from a defective interaction of the chimeric protein with the export machinery. We have characterized suppressors which map in secG, a newly defined gene of the export machinery. All single amino acid substitutions map to three adjacent codons. These secG mutants have a weak Sec phenotype, as determined by their effect on export mediated by wild-type and mutant signal sequences. Whilst a secG disruption allele also confers a weak Sec phenotype, it does not suppress the toxicity of the chimeric protein. This difference results from a selective effect of the secG suppressors on the kinetics of export mediated by the PAI-2 signal sequence. Using a malE signal sequence mutant, which has a Mal-phenotype in secG mutant strains, we have isolated extragenic Mal+ suppressors. Most suppressors map to secY, and several are allele-specific. Finally, SecG overexpression accelerates the kinetics of protein export, suggesting that there are two types of functional translocation complexes: with or without SecG.

Indexed as

ATP-Binding Cassette TransportersEscherichia coli ProteinsMonosaccharide Transport ProteinsPeriplasmic Binding ProteinsSuppression, GeneticAlkaline PhosphataseAmino Acid SequenceBacterial Outer Membrane ProteinsBacterial ProteinsBase SequenceBiological TransportCarrier ProteinsChromosome MappingEscherichia coliImmunoblottingMaltose-Binding ProteinsAlkaline PhosphataseATP-Binding Cassette TransportersBacterial Outer Membrane ProteinsBacterial ProteinsCarrier ProteinsEscherichia coli ProteinsMalE protein, E coliMaltose-Binding Proteinsmaltose transport system, E coliMembrane ProteinsMonosaccharide Transport ProteinsPeriplasmic Binding ProteinsPlasminogen Activator Inhibitor 2SecG protein, E coliSEC Translocation ChannelsSecY protein, E coli

Identifiers

PMID7556084
PMCPMC394532
OpenAlexW1587008866

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.