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

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dc.contributor.author Kthiri, Fatoum
dc.contributor.author Le, Hai-Tuong
dc.contributor.author Tagourti, Jihen
dc.contributor.author Kern, Renee
dc.contributor.author Malki, Abderrahim
dc.contributor.author Caldas, Teresa
dc.contributor.author Abdallah, Jad
dc.contributor.author Landoulsi, Ahmed
dc.contributor.author Richarme, Gilbert
dc.date.accessioned 2016-07-19T09:38:32Z
dc.date.available 2016-07-19T09:38:32Z
dc.date.copyright 2008 en_US
dc.date.issued 2016-07-19
dc.identifier.issn 0006-291X en_US
dc.identifier.uri http://hdl.handle.net/10725/4166
dc.description.abstract 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-reductase and chaperone properties in vitro. In this study, we show that an ybbN-deficient strain displays an increased sensitivity to thermal stress but not to oxidative stress, a normal redox state of its cellular proteins but a decreased expression of several cytoplasmic proteins, including EF-Tu, DnaK, GroEL, trigger factor and several Krebs cycle enzymes, suggesting that the chaperone properties of YbbN are more important in vivo than its redox properties. YbbN specifically interacts with DnaK and GroEL, as shown by reverse purification. It increases 4-fold the rate of protein renaturation in vitro by the DnaK chaperone machine, suggesting that it cooperates with DnaK for the optimal expression of several cytoplasmic proteins. en_US
dc.language.iso en en_US
dc.title The thioredoxin homolog YbbN functions as a chaperone rather than as an oxidoreductase en_US
dc.type Article en_US
dc.description.version Published en_US
dc.author.school SOP en_US
dc.author.idnumber 200703820 en_US
dc.author.department Pharmaceutical Sciences Department en_US
dc.description.embargo N/A en_US
dc.relation.journal Biochemical and Biophysical Research Communications en_US
dc.journal.volume 374 en_US
dc.journal.issue 4 en_US
dc.article.pages 668-672 en_US
dc.keywords YbbN en_US
dc.keywords Thioredoxin en_US
dc.keywords Chaperone en_US
dc.keywords Oxidoreductase en_US
dc.keywords SXXC en_US
dc.keywords Heat stress en_US
dc.keywords Oxidative stress en_US
dc.keywords Bacteria en_US
dc.identifier.doi http://dx.doi.org/10.1016/j.bbrc.2008.07.080 en_US
dc.identifier.ctation Kthiri, F., Le, H. T., Tagourti, J., Kern, R., Malki, A., Caldas, T., ... & Richarme, G. (2008). The thioredoxin homolog YbbN functions as a chaperone rather than as an oxidoreductase. Biochemical and biophysical research communications, 374(4), 668-672. en_US
dc.author.email jabdallah@lau.edu.lb en_US
dc.identifier.tou http://libraries.lau.edu.lb/research/laur/terms-of-use/articles.php en_US
dc.identifier.url http://www.sciencedirect.com/science/article/pii/S0006291X08014198 en_US
dc.orcid.id https://orcid.org/0000-0001-5267-4953 en_US

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