Evidence map›Paper›PMID 25385585›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Interacting cytoplasmic loops of subunits a and c of Escherichia coli F1F0 ATP synthase gate H+ transport to the cytoplasm.

P Ryan Steed, Kaitlin A Kraft, Robert H Fillingame

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.1field-weighted citation impact, top 46% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. Review
  2. 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.

P Ryan SteedDepartment of Biomolecular Chemistry, University of Wisconsin School Medicine and Public Health, Madison, WI 53706-1532.
Kaitlin A KraftDepartment of Biomolecular Chemistry, University of Wisconsin School Medicine and Public Health, Madison, WI 53706-1532.
Robert H FillingameDepartment of Biomolecular Chemistry, University of Wisconsin School Medicine and Public Health, Madison, WI 53706-1532 rhfillin@wisc.edu.
University of Wisconsin–Madison · US

Funding

Proton-Translocating Sector of E. coli H+ATP SynthaseR01GM023105 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI FILLINGAME, ROBERT H · 1985 to 2010
$2.5M
PROTON-TRANSLOCATING SECTOR OF E COLI H+ ATPASER37GM023105 · NIGMS · UNIVERSITY OF WISCONSIN MADISON · PI FILLINGAME, ROBERT H · 1994 to 2003
$1.8M
NIGMS NIH HHS GM23105NIGMS NIH HHS R01 GM023105NIGMS NIH HHS R37 GM023105
6 · The paper itself

Abstract

H(+)-transporting F1F0 ATP synthase catalyzes the synthesis of ATP via coupled rotary motors within F0 and F1. H(+) transport at the subunit a-c interface in transmembranous F0 drives rotation of a cylindrical c10 oligomer within the membrane, which is coupled to rotation of subunit γ within the α3β3 sector of F1 to mechanically drive ATP synthesis. F1F0 functions in a reversible manner, with ATP hydrolysis driving H(+) transport. ATP-driven H(+) transport in a select group of cysteine mutants in subunits a and c is inhibited after chelation of Ag(+) and/or Cd(+2) with the substituted sulfhydryl groups. The H(+) transport pathway mapped via these Ag(+)(Cd(+2))-sensitive Cys extends from the transmembrane helices (TMHs) of subunits a and c into cytoplasmic loops connecting the TMHs, suggesting these loop regions could be involved in gating H(+) release to the cytoplasm. Here, using select loop-region Cys from the single cytoplasmic loop of subunit c and multiple cytoplasmic loops of subunit a, we show that Cd(+2) directly inhibits passive H(+) transport mediated by F0 reconstituted in liposomes. Further, in extensions of previous studies, we show that the regions mediating passive H(+) transport can be cross-linked to each other. We conclude that the loop-regions in subunits a and c that are implicated in H(+) transport likely interact in a single structural domain, which then functions in gating H(+) release to the cytoplasm.

Indexed as

Biological TransportCadmiumCytoplasmEscherichia coliMitochondrial Proton-Translocating ATPasesProtonsSilverCadmiumF1F0-ATP synthaseMitochondrial Proton-Translocating ATPasesProtonsSilverF0 a–c subunitsF0 half channelsF1F0 ATP synthasegating mechanismproton transport

Identifiers

PMID25385585
PMCPMC4250104
OpenAlexW2031680224

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.