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| Content Provider | Springer Nature Link |
|---|---|
| Author | Madonna, Stefania Papa, Rosanna Birolo, Leila Autore, Flavia Doti, Nunzianna Mari, Gennaro Quemeneur, Eric Sannia, Giovanni Tuti, Maria L. Duilio, Angela |
| Copyright Year | 2005 |
| Abstract | In prokaryotes, protein disulfide bond oxidation, reduction and isomerization are catalyzed by members of the thioredoxin superfamily, characterized by the conserved C–X–X–C motif in their active site. Thioredoxins and glutaredoxins contribute to the reducing power in the cytoplasm, while the Dsb system catalyzes disulfide bonds formation in the periplasmic space.This paper addresses the question of disulfide bonds formation in a cold-adapted micro-organism, Pseudoalteromonas haloplanktis TAC 125 (PhTAC125) by characterizing the DsbA system. We found distinctive features respect mesophilic counterparts that highlighted for the first time the occurrence of two adjacent chromosomal DsbA genes organised in a functional operon. The sophisticated transcriptional regulation mechanism that controls the expression of these two genes was also defined. The two DsbA proteins, named PhDsbA and PhDsbA2, respectively, were expressed in Escherichia coli and characterized.Results reported in this paper provide some insights into disulfide bonds formation in a micro organism isolated in the Antarctic sea water. |
| Starting Page | 41 |
| Ending Page | 51 |
| Page Count | 11 |
| File Format | |
| ISSN | 14310651 |
| Journal | Extremophiles |
| Volume Number | 10 |
| Issue Number | 1 |
| e-ISSN | 14334909 |
| Language | English |
| Publisher | Springer-Verlag |
| Publisher Date | 2005-09-23 |
| Publisher Place | Tokyo |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Pseudoalteromonas haloplanktis Gene regulation Cold adaptation Thiol disulfide oxidoreductase pathways Protein folding DsbA |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Molecular Medicine Microbiology |
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