Escherchia coli ribose binding protein based bioreporters revisited.

Détails

Ressource 1Télécharger: BIB_81FA3F0E8394.P001.pdf (1757.49 [Ko])
Etat: Serval
Version: Author's accepted manuscript
ID Serval
serval:BIB_81FA3F0E8394
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Escherchia coli ribose binding protein based bioreporters revisited.
Périodique
Scientific Reports
Auteur(s)
Reimer A., Yagur-Kroll S., Belkin S., Roy S., van der Meer J.R.
ISSN
2045-2322 (Electronic)
ISSN-L
2045-2322
Statut éditorial
Publié
Date de publication
2014
Volume
4
Pages
5626
Langue
anglais
Résumé
Bioreporter bacteria, i.e., strains engineered to respond to chemical exposure by production of reporter proteins, have attracted wide interest because of their potential to offer cheap and simple alternative analytics for specified compounds or conditions. Bioreporter construction has mostly exploited the natural variation of sensory proteins, but it has been proposed that computational design of new substrate binding properties could lead to completely novel detection specificities at very low affinities. Here we reconstruct a bioreporter system based on the native Escherichia coli ribose binding protein RbsB and one of its computationally designed variants, reported to be capable of binding 2,4,6-trinitrotoluene (TNT). Our results show in vivo reporter induction at 50 nM ribose, and a 125 nM affinity constant for in vitro ribose binding to RbsB. In contrast, the purified published TNT-binding variant did not bind TNT nor did TNT cause induction of the E. coli reporter system.
Pubmed
Web of science
Création de la notice
25/01/2015 16:46
Dernière modification de la notice
03/03/2018 18:49
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