The NMR signature of gluconoylation: a frequent N-terminal modification of isotope-labeled proteins View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2019-02

AUTHORS

David Schweida, Pierre Barraud, Christof Regl, Fionna E. Loughlin, Christian G. Huber, Chiara Cabrele, Mario Schubert

ABSTRACT

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 13C/15N labeled proteins, their chemical shifts were not yet reported. Here we present the complete 1H and 13C chemical shift assignment of the N-terminal gluconoyl post-translational modification, based on a selection of His-tagged protein constructs (CCL2, hnRNP A1 and Lin28) starting with Met-Gly-...-(His)6. In addition, we show that the modification can hydrolyze over time, resulting in a free N-terminus and gluconate. This leads to the disappearance of the gluconoyl signals and the appearance of gluconate signals during the NMR measurements. The chemical shifts presented here can now be used as a reference for the identification of gluconoylation in recombinant proteins, in particular when isotopically labeled. More... »

PAGES

71-79

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s10858-019-00228-6

DOI

http://dx.doi.org/10.1007/s10858-019-00228-6

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1112020493

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30737614


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