Evidence map›Paper›PMID 10369667›Full record

ArticleThe EMBO journal1999

The PrlA and PrlG phenotypes are caused by a loosened association among the translocase SecYEG subunits.

F Duong, W Wickner

Abstract read
In one paragraph

Article in The EMBO journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
4.8field-weighted citation impact, top 5% 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

36 citing papers in PubMed, 77 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Protein export through the bacterial Sec pathway.Nature reviews. Microbiology · 2017
    Review
  8. Article
  9. Unlocking the Bacterial SecY Translocon.Structure (London, England : 1993) · 2016
    Article
  10. Article
  11. Article
  12. Article
  13. Emerging themes in SecA2-mediated protein export.Nature reviews. Microbiology · 2012
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. SecA, a remarkable nanomachine.Cellular and molecular life sciences : CMLS · 2011
    Review
  20. Probing the SecYEG translocation pore size with preproteins conjugated with sizable rigid spherical molecules.Proceedings of the National Academy of Sciences of the United States of America · 2011
    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 2 countries.

F DuongLaboratoire Transports et Signalisation Cellulaires, CNRS UMR 8619, Bâtiment 430, Université de Paris XI, Orsay, 91405, France.
W Wickner
Université Paris Cité · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

prlA mutations in the gene encoding the SecY subunit of the membrane domain of the Escherichia coli preprotein translocase confer many phenotypes: enhanced translocation rates, increased affinity for SecA, diminished requirement for functional leader sequences, reduced proton-motive force (PMF) dependence of preprotein translocation and facilitated translocation of preproteins with folded domains. We now report that both prlA and prlG mutations weaken the associations between the SecY, SecE and SecG subunits of the translocase. This loosened association increases the initiation of translocation by facilitating the insertion of SecA with its bound preprotein but reduces the stimulatory effect of the PMF during the initial step of translocation. Furthermore, the originally isolated prlA4 mutant, which possesses a particularly labile SecYEG complex, acquired a secondary mutation that restored the stability while conserving the flexibility of the complex. Combinations of certain prlA and prlG mutations, known to cause synthetic lethality in vivo, dramatically loosen subunit association and lead to complete disassembly of SecYEG. These findings underscore the importance of the loosened SecYEG association for the Prl phenotypes. We propose a model in which each of the PrlA and PrlG phenotypes derive from this enhanced SecYEG conformational flexibility.

Indexed as

Escherichia coli ProteinsMembrane Transport ProteinsAdenosine TriphosphatasesAllelesBacterial ProteinsBiological TransportEscherichia coliGenes, SuppressorMembrane ProteinsModels, BiologicalMutationPhenotypeProtein BindingProtein ConformationProtein PrecursorsProton-Motive ForceAdenosine TriphosphatasesBacterial ProteinsEscherichia coli ProteinsMembrane ProteinsMembrane Transport ProteinsProtein PrecursorsSecA ProteinsSecE protein, E coliSecG protein, E coliSEC Translocation ChannelsSecY protein, E coli

Identifiers

PMID10369667
PMCPMC1171407
OpenAlexW2097534440

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.