The thioredoxin homolog YbbN functions as a chaperone rather than as an oxidoreductase

The thioredoxin homolog YbbN functions as a chaperone rather than as an oxidoreductase

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 20 kDa C-terminal part of unknown function. We reported previously that YbbN displays both protein oxido-reducta...

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Bibliographic Details
Main Author: Kthiri, Fatoum (author)
Other Authors: Le, Hai-Tuong (author), Tagourti, Jihen (author), Kern, Renee (author), Malki, Abderrahim (author), Caldas, Teresa (author), Abdallah, Jad (author), Landoulsi, Ahmed (author), Richarme, Gilbert (author)
Format: article
Published: 2008
Online Access:http://hdl.handle.net/10725/4166
http://dx.doi.org/10.1016/j.bbrc.2008.07.080
http://libraries.lau.edu.lb/research/laur/terms-of-use/articles.php
http://www.sciencedirect.com/science/article/pii/S0006291X08014198
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http://hdl.handle.net/10725/4166
http://dx.doi.org/10.1016/j.bbrc.2008.07.080
http://libraries.lau.edu.lb/research/laur/terms-of-use/articles.php
http://www.sciencedirect.com/science/article/pii/S0006291X08014198

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