Evidence map›Paper›PMID 8083155›Full record

ArticleJournal of bacteriology1994

PrlA and PrlG suppressors reduce the requirement for signal sequence recognition.

A M Flower, R C Doebele, T J Silhavy

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

33 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. The bacterial Sec-translocase: structure and mechanism.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. SPdb--a signal peptide database.BMC bioinformatics · 2005
    Article
  15. Article
  16. Article
  17. Review
  18. Ring-like pore structures of SecA: implication for bacterial protein-conducting channels.Proceedings of the National Academy of Sciences of the United States of America · 2003
    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

3 authors at 1 institution in 1 country.

A M FlowerDepartment of Molecular Biology, Princeton University, New Jersey 08544.
R C Doebele
T J Silhavy
Princeton University · US

Funding

GENETIC ANALYSIS OF PROTEIN EXPORTR37GM034821 · NIGMS · PRINCETON UNIVERSITY · PI SILHAVY, THOMAS J. · 1999 to 2008
$4.9M
GENETIC ANALYSIS OF PROTEIN EXPORTR01GM034821 · NIGMS · PRINCETON UNIVERSITY · PI SILHAVY, THOMAS J. · 1985 to 2015
$4.7M
NIGMS NIH HHS GM14138NIGMS NIH HHS GM34821
6 · The paper itself

Abstract

Selection for suppressors of defects in the signal sequence of secretory proteins has led most commonly to identification of prlA alleles and less often to identification of prlG alleles. These genes, secY/prlA and secE/prlG, encode integral membrane components of the protein translocation system of Escherichia coli. We demonstrate that an outer membrane protein, LamB, that lacks a signal sequence can be exported with reasonable efficiency in both prlA and prlG suppressor strains. Although the signal sequence is not absolutely required for export of LamB, the level of export in the absence of prl suppressor alleles is exceedingly low. Such strains are phenotypically LamB-, and functional LamB can be detected only by using sensitive infectious-center assays. Suppression of the LamB signal sequence deletion is dependent on normal components of the export pathway, indicating that suppression is not occurring through a bypass mechanism. Our results indicate that the majority of the known prlA suppressors function by an identical mechanism and, further, that the prlG suppressors work in a similar fashion. We propose that both PrlA and PrlG suppressors lack a proofreading activity that normally rejects defective precursors from the export pathway.

Indexed as

Escherichia coli ProteinsBacterial Outer Membrane ProteinsBacterial ProteinsDNA Mutational AnalysisEscherichia coliGenes, BacterialGenes, SuppressorMembrane ProteinsPorinsProtein ConformationProtein Sorting SignalsReceptors, VirusSEC Translocation ChannelsSequence DeletionBacterial Outer Membrane ProteinsBacterial ProteinsEscherichia coli ProteinsmaltoporinsMembrane ProteinsPorinsProtein Sorting SignalsReceptors, VirusSecE protein, E coliSEC Translocation ChannelsSecY protein, E coli

Identifiers

PMID8083155
PMCPMC196762
OpenAlexW2121689536

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.