Evidence map›Paper›PMID 26522884›Full record

ArticleChembiochem : a European journal of chemical biology2016

N-Lauroylation during the Expression of Recombinant N-Myristoylated Proteins: Implications and Solutions.

Andrea Gabriele Flamm, Anabel-Lise Le Roux, Borja Mateos, Mireia Díaz-Lobo, Barbara Storch, Kathrin Breuker, Robert Konrat, Miquel Pons, Nicolas Coudevylle

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In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2016. 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
–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

2 citing papers in PubMed.

  1. Article
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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

9 authors.

Andrea Gabriele FlammDepartment of Computational and Structural Biology, F. Max Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, 1030, Vienna, Austria.
Anabel-Lise Le RouxBiomolecular NMR Laboratory, Department of Organic Chemistry, University of Barcelona, Baldiri Reixac 10-12, 08028, Barcelona, Spain.
Borja MateosBiomolecular NMR Laboratory, Department of Organic Chemistry, University of Barcelona, Baldiri Reixac 10-12, 08028, Barcelona, Spain.
Mireia Díaz-LoboInstitute for Research in Biomedicine (IRB Barcelona), Baldiri Reixac 10-12, 08028, Barcelona, Spain.
Barbara StorchInstitute of Organic Chemistry, Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck, CCB, Innrain 80/82, 6020, Innsbruck, Austria.
Kathrin BreukerInstitute of Organic Chemistry, Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck, CCB, Innrain 80/82, 6020, Innsbruck, Austria.
Robert KonratDepartment of Computational and Structural Biology, F. Max Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, 1030, Vienna, Austria.
Miquel PonsBiomolecular NMR Laboratory, Department of Organic Chemistry, University of Barcelona, Baldiri Reixac 10-12, 08028, Barcelona, Spain.
Nicolas CoudevylleDepartment of Computational and Structural Biology, F. Max Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, 1030, Vienna, Austria. nicolas.coudevylle@univie.ac.at.

Funding

Austrian Science Fund FWF P 26317Austrian Science Fund FWF P 27347Austrian Science Fund FWF Y 372
6 · The paper itself

Abstract

Incorporation of myristic acid onto the N terminus of a protein is a crucial modification that promotes membrane binding and correct localization of important components of signaling pathways. Recombinant expression of N-myristoylated proteins in Escherichia coli can be achieved by co-expressing yeast N-myristoyltransferase and supplementing the growth medium with myristic acid. However, undesired incorporation of the 12-carbon fatty acid lauric acid can also occur (leading to heterogeneous samples), especially when the available carbon sources are scarce, as it is the case in minimal medium for the expression of isotopically enriched samples. By applying this method to the brain acid soluble protein 1 and the 1-185 N-terminal region of c-Src, we show the significant, and protein-specific, differences in the membrane binding properties of lauroylated and myristoylated forms. We also present a robust strategy for obtaining lauryl-free samples of myristoylated proteins in both rich and minimal media.

Indexed as

Myristic AcidProteinsRecombinant ProteinsSolutionsMyristic AcidProteinsRecombinant ProteinsSolutionsintrinsically disordered proteinslauroylationmyristoylationsurface plasmon resonancetransferases

Identifiers

PMID26522884
PMCPMC4736449

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Registered trials

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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.