Article
The thioredoxin homolog YbbN functions as a chaperone rather than as an oxidoreductase.
Biochemical and biophysical research communications - 3 Oct 2008
Kthiri Fatoum, Le Hai-Tuong, Tagourti Jihen, Kern Renée, Malki Abderrahim, Caldas Teresa, Abdallah Jad, Landoulsi Ahmed, Richarme Gilbert
Abstract excerpt
Escherichia coli contains two thioredoxins, Trx1 and Trx2, and a thioredoxin-like protein, YbbN, which presents a strong homology in its N-terminal part with thioredoxins, and possesses a 20kDa C-terminal part of unknown function. We reported previously that YbbN displays both protein oxido-reductase and chaperone properties in vitro. In this study, we show that an ybbN-deficient strain displays an increased...
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