Evidence map›Paper›PMID 17588940›Full record

ArticleThe Journal of biological chemistry2007

Patch clamp and phenotypic analyses of a prokaryotic cyclic nucleotide-gated K+ channel using Escherichia coli as a host.

Mario Meng-Chiang Kuo, Yoshiro Saimi, Ching Kung, Senyon Choe

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

17 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
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  6. The application of theBiotechnology reports (Amsterdam, Netherlands) · 2015
    Article
  7. Family of prokaryote cyclic nucleotide-modulated ion channels.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  8. Article
  9. Article
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  12. Structure of the MthK RCK in complex with cadmium.Journal of structural biology · 2010
    Article
  13. Article
  14. Article
  15. Article
  16. Ion channels in microbes.Physiological reviews · 2008
    Review
  17. 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

4 authors at 2 institutions in 1 country.

Mario Meng-Chiang KuoStructural Biology Laboratory, The Salk Institute, La Jolla, California 92037, USA.
Yoshiro Saimi
Ching Kung
Senyon Choe
Salk Institute for Biological Studies · USUniversity of Wisconsin–Madison · US

Funding

Study of mechanosensation using microbial TRP channelsR01GM047856 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI KUNG, CHING · 1994 to 2008
$2.2M
Molecular Basis of Hypertonicity Sensing by Yeast Yvc1pR01GM054867 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI KUNG, CHING · 1998 to 2010
$2.2M
Structures of Eukaryotic K Channels and Mistic ActionR01GM074821 · NIGMS · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI CHOE, SENYON · 2005 to 2008
$1.5M
NIGMS NIH HHS GM047856NIGMS NIH HHS GM054867NIGMS NIH HHS GM74821NIGMS NIH HHS R01 GM047856NIGMS NIH HHS R01 GM054867NIGMS NIH HHS R01 GM074821
6 · The paper itself

Abstract

Prokaryotic ion channels have been valuable in providing structural models for understanding ion filtration and channel-gating mechanisms. However, their functional examinations have remained rare and usually been carried out by incorporating purified channel protein into artificial lipid membranes. Here we demonstrate the utilization of Escherichia coli to host the functional analyses by examining a putative cyclic nucleotide-gated K+ channel cloned from Magnetospirillum magnetotacticum, MmaK. When expressed in wild-type E. coli cells, MmaK renders the host sensitive to millimolar concentrations of externally applied K+, indicating MmaK forms a functional K+ conduit in the E. coli membrane in vivo. After enlarging these cells into giant spheroplasts, macro- and microscopic MmaK currents are readily detected in excised E. coli membrane patches by a patch clamp. We show that MmaK is indeed gated by submicromolar cAMP and approximately 10-fold higher concentration of cGMP and manifests as an inwardly rectified, K+-specific current with a 10.8 pS unitary conductance at -100 mV. Additionally, MmaK is inactivated by slightly acidic pH only from the cytoplasmic side. Our in vitro biophysical characterizations of MmaK correlate with its in vivo phenotype in E. coli, implicating its critical role as an intracellular cAMP and pH sensor for modulating bacterial membrane potential. Exemplified by MmaK functional studies, we establish that E. coli and its giant spheroplast provide a convenient and versatile system to express foreign channels for biophysical analyses that can be further dovetailed with microbial genetics.

Indexed as

Bacterial ProteinsCloning, MolecularCyclic Nucleotide-Gated Cation ChannelsElectrophysiologyEscherichia coliIon ChannelsMagnetospirillumPatch-Clamp TechniquesPotassium ChannelsBacterial ProteinsCyclic Nucleotide-Gated Cation ChannelsIon ChannelsPotassium Channels

Identifiers

PMID17588940
PMCPMC3521034
OpenAlexW1965031043

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.