The NMR signature of gluconoylation: a frequent N-terminal modification of isotope-labeled proteins.

E. coli Gluconic acid Gluconoylation N-terminus NMR spectroscopy Post-translational protein modification Recombinant protein

Journal

Journal of biomolecular NMR
ISSN: 1573-5001
Titre abrégé: J Biomol NMR
Pays: Netherlands
ID NLM: 9110829

Informations de publication

Date de publication:
Feb 2019
Historique:
received: 22 12 2018
accepted: 24 01 2019
pubmed: 10 2 2019
medline: 30 4 2019
entrez: 10 2 2019
Statut: ppublish

Résumé

N-terminal gluconoylation is a moderately widespread modification in recombinant proteins expressed in Escherichia coli, in particular in proteins bearing an N-terminal histidine-tag. This post-translational modification has been investigated mainly by mass spectrometry. Although its NMR signals must have been observed earlier in spectra of

Identifiants

pubmed: 30737614
doi: 10.1007/s10858-019-00228-6
pii: 10.1007/s10858-019-00228-6
pmc: PMC6441400
doi:

Substances chimiques

Gluconates 0
Recombinant Proteins 0
gluconic acid R4R8J0Q44B

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

71-79

Références

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Auteurs

David Schweida (D)

Department of Biosciences, University of Salzburg, Billrothstr. 11, 5020, Salzburg, Austria.

Pierre Barraud (P)

Institute of Molecular Biology and Biophysics, ETH Zürich, 8093, Zurich, Switzerland.
Institut de Biologie Physico-Chimique (IBPC), UMR 8261 CNRS, Université Paris Diderot, 13 rue Pierre et Marie Curie, 75005, Paris, France.

Christof Regl (C)

Department of Biosciences, University of Salzburg, Billrothstr. 11, 5020, Salzburg, Austria.
Christian Doppler Laboratory for Innovative Tools for Biosimilar Characterization, University of Salzburg, Hellbrunnerstrasse 34, 5020, Salzburg, Austria.

Fionna E Loughlin (FE)

Institute of Molecular Biology and Biophysics, ETH Zürich, 8093, Zurich, Switzerland.
Department of Biochemistry & Molecular Biology, Monash Biomedicine Discovery Institute, Monash University, Clayton, VIC, 3800, Australia.

Christian G Huber (CG)

Department of Biosciences, University of Salzburg, Billrothstr. 11, 5020, Salzburg, Austria.
Christian Doppler Laboratory for Innovative Tools for Biosimilar Characterization, University of Salzburg, Hellbrunnerstrasse 34, 5020, Salzburg, Austria.

Chiara Cabrele (C)

Department of Biosciences, University of Salzburg, Billrothstr. 11, 5020, Salzburg, Austria.
Christian Doppler Laboratory for Innovative Tools for Biosimilar Characterization, University of Salzburg, Hellbrunnerstrasse 34, 5020, Salzburg, Austria.

Mario Schubert (M)

Department of Biosciences, University of Salzburg, Billrothstr. 11, 5020, Salzburg, Austria. mario.schubert@sbg.ac.at.
Institute of Molecular Biology and Biophysics, ETH Zürich, 8093, Zurich, Switzerland. mario.schubert@sbg.ac.at.
Christian Doppler Laboratory for Innovative Tools for Biosimilar Characterization, University of Salzburg, Hellbrunnerstrasse 34, 5020, Salzburg, Austria. mario.schubert@sbg.ac.at.

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Classifications MeSH