Evidence map›Paper›PMID 18059473›Full record

ArticleThe EMBO journal2008

Parallel topology of genetically fused EmrE homodimers.

Sonia Steiner-Mordoch, Misha Soskine, Dalia Solomon, Dvir Rotem, Ayala Gold, Michal Yechieli, Yoav Adam, Shimon Schuldiner

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

20 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Single-Molecule FRET of Membrane Transport Proteins.Chembiochem : a European journal of chemical biology · 2021
    Review
  3. Article
  4. Stable membrane orientations of small dual-topology membrane proteins.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Analyzing conformational changes in the transport cycle of EmrE.Current opinion in structural biology · 2012
    Review
  11. Article
  12. Article
  13. Structural perspectives on secondary active transporters.Trends in pharmacological sciences · 2010
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. An emerging consensus for the structure of EmrE.Acta crystallographica. Section D, Biological crystallography · 2009
    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

8 authors at 1 institution in 1 country.

Sonia Steiner-MordochDepartment of Biological Chemistry, Alexander Silberman Institute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem, Israel.
Misha Soskine
Dalia Solomon
Dvir Rotem
Ayala Gold
Michal Yechieli
Yoav Adam
Shimon Schuldiner
Hebrew University of Jerusalem · IL

Funding

MOLECULAR MECHANISM OF ACTIVE NEUROTRANSMITTER TRANSPORTR01NS016708 · NINDS · HEBREW UNIVERSITY OF JERUSALEM · PI KANNER, BARUCH I, SCHULDINER, SHIMON · 1985 to 2014
$3.0M
Mechanisms of Active Neurotransmitter TransportR56NS016708 · NINDS · HEBREW UNIVERSITY OF JERUSALEM · PI KANNER, BARUCH I, SCHULDINER, SHIMON · 2009 to 2009
$306k
NINDS NIH HHS NS16708NINDS NIH HHS R01 NS016708NINDS NIH HHS R56 NS016708
6 · The paper itself

Abstract

EmrE is a small H+-coupled multidrug transporter in Escherichia coli. Claims have been made for an antiparallel topology of this homodimeric protein. However, our own biochemical studies performed with detergent-solubilized purified protein support a parallel topology of the protomers. We developed an alternative approach to constrain the relative topology of the protomers within the dimer so that their activity can be assayed also in vivo before biochemical handling. Tandem EmrE was built with two identical monomers genetically fused tail to head (C-terminus of the first to N-terminus of the second monomer) with hydrophilic linkers of varying length. All the constructs conferred resistance to ethidium by actively removing it from the cytoplasm. The purified proteins bound substrate and transported methyl viologen into proteoliposomes by a proton-dependent mechanism. A tandem where one of the essential glutamates was replaced with glutamine transported only monovalent substrates and displayed a modified stoichiometry. The results support a parallel topology of the protomers in the functional dimer. The implications regarding insertion and evolution of membrane proteins are discussed.

Indexed as

Amino Acid SequenceAntiportersBiological Transport, ActiveCytoplasmDimerizationDrug Resistance, Multiple, BacterialElectron TransportEscherichia coliEscherichia coli ProteinsEthidiumMembrane ProteinsMolecular Sequence DataProtein Structure, SecondaryRecombinant Fusion ProteinsSubstrate SpecificityThermodynamicsAntiportersEmrE protein, E coliEscherichia coli ProteinsEthidiumMembrane ProteinsRecombinant Fusion Proteins

Identifiers

PMID18059473
PMCPMC2206133
OpenAlexW2117745680

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.