Evidence map›Paper›PMID 27524616›Full record

ArticleCell reports2016

A Link between Integral Membrane Protein Expression and Simulated Integration Efficiency.

Stephen S Marshall, Michiel J M Niesen, Axel Müller, Katrin Tiemann, Shyam M Saladi, Rachel P Galimidi, Bin Zhang, William M Clemons, Thomas F Miller

Abstract read
In one paragraph

Article in Cell reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
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

11 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Producing membrane proteins one simulation at a time.The Journal of biological chemistry · 2017
    Article
  10. Article
  11. 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

9 authors.

Stephen S MarshallDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.
Michiel J M NiesenDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.
Axel MüllerDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.
Katrin TiemannDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.
Shyam M SaladiDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.
Rachel P GalimidiDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.
Bin ZhangDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.
William M ClemonsDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA. Electronic address: clemons@caltech.edu.
Thomas F MillerDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA. Electronic address: tfm@caltech.edu.

Funding

PREDOCTORAL TRAINING IN BIOLOGY AND CHEMISTRYT32GM007616 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI STERNBERG, PAUL WARREN · 1985 to 2019
$22.9M
NIH Pioneer AwardDP1GM105385 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI CLEMONS, WILLIAM M. · 2012 to 2015
$3.3M
NIGMS NIH HHS DP1 GM105385NIGMS NIH HHS T32 GM007616
6 · The paper itself

Abstract

Integral membrane proteins (IMPs) control the flow of information and nutrients across cell membranes, yet IMP mechanistic studies are hindered by difficulties in expression. We investigate this issue by addressing the connection between IMP sequence and observed expression levels. For homologs of the IMP TatC, observed expression levels vary widely and are affected by small changes in protein sequence. The effect of sequence changes on experimentally observed expression levels strongly correlates with the simulated integration efficiency obtained from coarse-grained modeling, which is directly confirmed using an in vivo assay. Furthermore, mutations that improve the simulated integration efficiency likewise increase the experimentally observed expression levels. Demonstration of these trends in both Escherichia coli and Mycobacterium smegmatis suggests that the results are general to other expression systems. This work suggests that IMP integration is a determinant for successful expression, raising the possibility of controlling IMP expression via rational design.

Indexed as

Gene Expression Regulation, BacterialAmino Acid SequenceCell MembraneCloning, MolecularEscherichia coliEscherichia coli ProteinsMembrane ProteinsMembrane Transport ProteinsModels, MolecularMycobacterium smegmatisProtein Conformation, alpha-HelicalProtein Interaction Domains and MotifsRecombinant ProteinsSequence AlignmentSequence Homology, Amino AcidEscherichia coli ProteinsMembrane ProteinsMembrane Transport ProteinsRecombinant ProteinsTatC protein, E coli

Identifiers

PMID27524616
PMCPMC5001948

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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.