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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| مؤلفون آخرون: | , , , , , , , |
| التنسيق: | article |
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2008
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| الوصول للمادة أونلاين: | 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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| _version_ | 1864513462934175744 |
|---|---|
| author | Kthiri, Fatoum |
| author2 | Le, Hai-Tuong Tagourti, Jihen Kern, Renee Malki, Abderrahim Caldas, Teresa Abdallah, Jad Landoulsi, Ahmed Richarme, Gilbert |
| author2_role | author author author author author author author author |
| author_facet | Kthiri, Fatoum Le, Hai-Tuong Tagourti, Jihen Kern, Renee Malki, Abderrahim Caldas, Teresa Abdallah, Jad Landoulsi, Ahmed Richarme, Gilbert |
| author_role | author |
| dc.creator.none.fl_str_mv | Kthiri, Fatoum Le, Hai-Tuong Tagourti, Jihen Kern, Renee Malki, Abderrahim Caldas, Teresa Abdallah, Jad Landoulsi, Ahmed Richarme, Gilbert |
| dc.date.none.fl_str_mv | 2008 2016-07-19T09:38:32Z 2016-07-19T09:38:32Z 2016-07-19 |
| dc.identifier.none.fl_str_mv | 0006-291X http://hdl.handle.net/10725/4166 http://dx.doi.org/10.1016/j.bbrc.2008.07.080 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. http://libraries.lau.edu.lb/research/laur/terms-of-use/articles.php http://www.sciencedirect.com/science/article/pii/S0006291X08014198 |
| dc.language.none.fl_str_mv | en |
| dc.relation.none.fl_str_mv | Biochemical and Biophysical Research Communications |
| dc.rights.*.fl_str_mv | info:eu-repo/semantics/openAccess |
| dc.title.none.fl_str_mv | The thioredoxin homolog YbbN functions as a chaperone rather than as an oxidoreductase |
| dc.type.none.fl_str_mv | Article info:eu-repo/semantics/publishedVersion info:eu-repo/semantics/article |
| description | 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. |
| eu_rights_str_mv | openAccess |
| format | article |
| id | LAURepo_ce894dcb6fcb775ee0b4e4391953140c |
| identifier_str_mv | 0006-291X 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. |
| language_invalid_str_mv | en |
| network_acronym_str | LAURepo |
| network_name_str | Lebanese American University repository |
| oai_identifier_str | oai:laur.lau.edu.lb:10725/4166 |
| publishDate | 2008 |
| repository.mail.fl_str_mv | |
| repository.name.fl_str_mv | |
| repository_id_str | |
| spelling | The thioredoxin homolog YbbN functions as a chaperone rather than as an oxidoreductaseKthiri, FatoumLe, Hai-TuongTagourti, JihenKern, ReneeMalki, AbderrahimCaldas, TeresaAbdallah, JadLandoulsi, AhmedRicharme, GilbertEscherichia 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.PublishedN/A2016-07-19T09:38:32Z2016-07-19T09:38:32Z20082016-07-19Articleinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article0006-291Xhttp://hdl.handle.net/10725/4166http://dx.doi.org/10.1016/j.bbrc.2008.07.080Kthiri, 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.http://libraries.lau.edu.lb/research/laur/terms-of-use/articles.phphttp://www.sciencedirect.com/science/article/pii/S0006291X08014198enBiochemical and Biophysical Research Communicationsinfo:eu-repo/semantics/openAccessoai:laur.lau.edu.lb:10725/41662021-03-19T10:03:23Z |
| spellingShingle | The thioredoxin homolog YbbN functions as a chaperone rather than as an oxidoreductase Kthiri, Fatoum |
| status_str | publishedVersion |
| title | The thioredoxin homolog YbbN functions as a chaperone rather than as an oxidoreductase |
| title_full | The thioredoxin homolog YbbN functions as a chaperone rather than as an oxidoreductase |
| title_fullStr | The thioredoxin homolog YbbN functions as a chaperone rather than as an oxidoreductase |
| title_full_unstemmed | The thioredoxin homolog YbbN functions as a chaperone rather than as an oxidoreductase |
| title_short | The thioredoxin homolog YbbN functions as a chaperone rather than as an oxidoreductase |
| title_sort | The thioredoxin homolog YbbN functions as a chaperone rather than as an oxidoreductase |
| url | 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 |