The Escherichia coli thioredoxin homolog YbbN/Trxsc is a chaperone and a weak protein oxidoreductase

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dc.contributor.author Caldas, Thérèse
dc.contributor.author Kern, Renee
dc.contributor.author Malki, Abderrahim
dc.contributor.author Abdallah, Jad
dc.contributor.author Richarme, Gilbert en_US
dc.date.accessioned 2016-07-19T09:16:11Z
dc.date.available 2016-07-19T09:16:11Z
dc.date.copyright 2006 en_US
dc.date.issued 2016-07-19
dc.identifier.issn 0006-291X en_US
dc.identifier.uri http://hdl.handle.net/10725/4164
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 thioredoxin 1 and 2. YbbN, however, does not possess the canonical Cys-x-x-Cys active site of thioredoxins, but instead a Ser-x-x-Cys site. In addition to Cys-38, located in the SxxC site, it contains a second cysteine, Cys-63, close to Cys-38 in the 3D model. Cys-38 and Cys-63 undergo an oxidoreduction process, suggesting that YbbN functions with two redox cysteines. Accordingly, YbbN catalyzes the oxidation of reduced RNase and the isomerization of scrambled RNase. Moreover, upon oxidation, its oligomeric state changes from dimers to tetramers and higher oligomers. YbbN also possesses chaperone properties, promoting protein folding after urea denaturation and forming complexes with unfolded proteins. This is the first biochemical characterization of a member of the YbbN class of bacterial thioredoxin-like proteins, and in vivo experiments will allow to determine the importance of its redox and chaperone properties in the cellular physiology. en_US
dc.language.iso en en_US
dc.title The Escherichia coli thioredoxin homolog YbbN/Trxsc is a chaperone and a weak protein 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 N/A 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 343 en_US
dc.journal.issue 3 en_US
dc.article.pages 780-786 en_US
dc.keywords YbbN en_US
dc.keywords Chaperone en_US
dc.keywords Oxidoreductase en_US
dc.keywords SxxC en_US
dc.keywords Heat shock en_US
dc.identifier.doi http://dx.doi.org/10.1016/j.bbrc.2006.03.028 en_US
dc.identifier.ctation Caldas, T., Malki, A., Kern, R., Abdallah, J., & Richarme, G. (2006). The Escherichia coli thioredoxin homolog YbbN/Trxsc is a chaperone and a weak protein oxidoreductase. Biochemical and biophysical research communications, 343(3), 780-786. 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/S0006291X06005274 en_US
dc.orcid.id https://orcid.org/0000-0001-5267-4953 en_US

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