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.
| Original language | English |
|---|---|
| Pages (from-to) | 41-51 |
| Number of pages | 11 |
| Journal | Extremophiles |
| Volume | 10 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Feb 2006 |
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Keywords
- Cold adaptation
- DsbA
- Gene regulation
- Protein folding
- Pseudoalteromonas haloplanktis
- Thiol disulfide oxidoreductase pathways
ASJC Scopus subject areas
- Applied Microbiology and Biotechnology
- Microbiology
Cite this
The thiol-disulfide oxidoreductase system in the cold-adapted bacterium Pseudoalteromonas haloplanktis TAC 125 : Discovery of a novel disulfide oxidoreductase enzyme. / Madonna, Stefania; Papa, Rosanna; Birolo, Leila; Autore, Flavia; Doti, Nunzianna; Marino, Gennaro; Quemeneur, Eric; Sannia, Giovanni; Tutino, Maria L.; Duilio, Angela.
In: Extremophiles, Vol. 10, No. 1, 02.2006, p. 41-51.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The thiol-disulfide oxidoreductase system in the cold-adapted bacterium Pseudoalteromonas haloplanktis TAC 125
T2 - Discovery of a novel disulfide oxidoreductase enzyme
AU - Madonna, Stefania
AU - Papa, Rosanna
AU - Birolo, Leila
AU - Autore, Flavia
AU - Doti, Nunzianna
AU - Marino, Gennaro
AU - Quemeneur, Eric
AU - Sannia, Giovanni
AU - Tutino, Maria L.
AU - Duilio, Angela
PY - 2006/2
Y1 - 2006/2
N2 - 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.
AB - 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.
KW - Cold adaptation
KW - DsbA
KW - Gene regulation
KW - Protein folding
KW - Pseudoalteromonas haloplanktis
KW - Thiol disulfide oxidoreductase pathways
UR - http://www.scopus.com/inward/record.url?scp=33644857162&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=33644857162&partnerID=8YFLogxK
U2 - 10.1007/s00792-005-0470-3
DO - 10.1007/s00792-005-0470-3
M3 - Article
C2 - 16179963
AN - SCOPUS:33644857162
VL - 10
SP - 41
EP - 51
JO - Extremophiles : life under extreme conditions
JF - Extremophiles : life under extreme conditions
SN - 1431-0651
IS - 1
ER -