Evidence map›Paper›PMID 8895565›Full record

ArticleThe EMBO journal1996

In vivo membrane assembly of the E.coli polytopic protein, melibiose permease, occurs via a Sec-independent process which requires the protonmotive force.

M Bassilana, C Gwizdek

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

9 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Membrane topology and insertion of membrane proteins: search for topogenic signals.Microbiology and molecular biology reviews : MMBR · 2000
    Review
  5. Article
  6. Membrane protein biogenesis: the exception explains the rules.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
  7. Linkage map of Escherichia coli K-12, edition 10: the traditional map.Microbiology and molecular biology reviews : MMBR · 1998
    Review
  8. Article
  9. 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.

M BassilanaLaboratoire J.Maetz, Departement de Biologie cellulaire et moléculairedu Commissariat à l'Energie Atomique, Villefranche-sur-mer, France.
C Gwizdek
Commissariat à l'Énergie Atomique et aux Énergies Alternatives · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To investigate the mechanism of polytopic membrane protein insertion in Escherichia coli, we have examined the protein and energy requirements for in vivo membrane assembly of the prototypic 12 transmembrane domain sugar co-transporter, melibiose permease (MelB). MelB membrane assembly was analyzed both kinetically, by pulse labeling experiments, and functionally by measuring the activity of the inserted permease. Strikingly, the rate of MelB membrane assembly is decreased approximately 4-fold upon dissipation of the transmembrane electrochemical proton gradient, delta(mu)H+, indicative of a strong requirement for delta(mu)H+. Interestingly, selective dissipation of either the electrical (delta(psi)) or the chemical (delta(pH)) component of delta(mu)H+ demonstrates that either form of energy is required for MelB membrane assembly. In contrast, MelB membrane assembly does not require SecA, SecY or SecE, all three proteins which are strictly required for protein translocation. Neither the rate of MelB membrane assembly nor the amount of functional permease is affected by inactivation or depletion of these Sec proteins. These results strongly suggest that polytopic membrane proteins such as MelB insert into the cytoplasmic membrane by a mechanism fundamentally different from protein translocation.

Indexed as

Escherichia coli ProteinsSymportersAdenosine TriphosphatasesAzidesBacterial Outer Membrane ProteinsBacterial ProteinsBiological TransportCarbonyl Cyanide m-Chlorophenyl HydrazoneCell MembraneEnzyme InhibitorsEscherichia coliGlucoseHydrogen-Ion ConcentrationKineticsMembrane Transport ProteinsMutationAdenosine TriphosphatasesAzidesBacterial Outer Membrane ProteinsBacterial ProteinsCarbonyl Cyanide m-Chlorophenyl HydrazoneEnzyme InhibitorsEscherichia coli ProteinsGlucosemelibiose permeaseMembrane Transport Proteinsouter membrane protein A precursor (E coli)Protein PrecursorsSecA ProteinsSecE protein, E coliSEC Translocation ChannelsSecY protein, E coliSodium AzideSymportersUncoupling Agents

Identifiers

PMID8895565
PMCPMC452264
OpenAlexW122626004

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.