Evidence map›Paper›PMID 26000747›Full record

ArticleChemistry & biology2015

The Effect of Detergent, Temperature, and Lipid on the Oligomeric State of MscL Constructs: Insights from Mass Spectrometry.

Eamonn Reading, Troy A Walton, Idlir Liko, Michael T Marty, Arthur Laganowsky, Douglas C Rees, Carol V Robinson

Open access · greenAbstract read
In one paragraph

Article in Chemistry & biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

51 citing papers in PubMed, 85 citations in OpenAlex.

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  10. Expanding Native Mass Spectrometry to the Masses.Journal of the American Society for Mass Spectrometry · 2024
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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

7 authors at 2 institutions in 2 countries.

Eamonn ReadingDepartment of Chemistry, Physical & Theoretical Chemistry Laboratory, University of Oxford, Oxford OX1 3TA, UK.
Troy A WaltonDivision of Chemistry and Chemical Engineering 114-96, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA.
Idlir LikoDepartment of Chemistry, Physical & Theoretical Chemistry Laboratory, University of Oxford, Oxford OX1 3TA, UK.
Michael T MartyDepartment of Chemistry, Physical & Theoretical Chemistry Laboratory, University of Oxford, Oxford OX1 3TA, UK.
Arthur LaganowskyDepartment of Chemistry, Physical & Theoretical Chemistry Laboratory, University of Oxford, Oxford OX1 3TA, UK.
Douglas C ReesDivision of Chemistry and Chemical Engineering 114-96, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA.
Carol V RobinsonDepartment of Chemistry, Physical & Theoretical Chemistry Laboratory, University of Oxford, Oxford OX1 3TA, UK. Electronic address: carol.robinson@chem.ox.ac.uk.
University of Oxford · GBCalifornia Institute of Technology · US

Funding

Biophysical, Structural and Functional Analysis of Mechanosensitive ChannelsR01GM084211 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI HASWELL, ELIZABETH S, PHILLIPS, ROB · 2008 to 2016
$3.6M
Medical Research Council 98101Medical Research Council G1000819NIGMS NIH HHS GM084211NIGMS NIH HHS R01 GM084211
6 · The paper itself

Abstract

The mechanosensitive channel of large conductance (MscL) acts as an emergency release valve for osmotic shock of bacteria preventing cell lysis. The large pore size, essential for function, requires the formation of oligomers with tetramers, pentamers, or hexamers observed depending on the species and experimental approach. We applied non-denaturing (native) mass spectrometry to five different homologs of MscL to determine the oligomeric state under more than 50 different experimental conditions elucidating lipid binding and subunit stoichiometry. We found equilibrium between pentameric and tetrameric species, which can be altered by detergent, disrupted by binding specific lipids, and perturbed by increasing temperature (37°C). We also established the presence of lipopolysaccharide bound to MscL and other membrane proteins expressed in Escherichia coli, revealing a potential source of heterogeneity. More generally, we highlight the use of mass spectrometry in probing membrane proteins under a variety of detergent-lipid environments relevant to structural biology.

Indexed as

Mass SpectrometryTemperatureAmino Acid SequenceBacterial ProteinsDetergentsEscherichia coliEscherichia coli ProteinsIon ChannelsLipidsLipopolysaccharidesMolecular Sequence DataProtein MultimerizationProtein Structure, QuaternaryRecombinant Fusion ProteinsSequence AlignmentBacterial ProteinsDetergentsEscherichia coli ProteinsIon ChannelsLipidsLipopolysaccharidesMscL protein, E coliRecombinant Fusion Proteins

Identifiers

PMID26000747
PMCPMC6585436
OpenAlexW2143904491

What OpenQuestion holds

Textmetadata
LicenceTDM
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.