The thiol-disulfide oxidoreductase system in the cold-adapted bacterium Pseudoalteromonas haloplanktis TAC 125: Discovery of a novel disulfide oxidoreductase enzyme

Stefania Madonna, Rosanna Papa, Leila Birolo, Flavia Autore, Nunzianna Doti, Gennaro Marino, Eric Quemeneur, Giovanni Sannia, Maria L. Tutino, Angela Duilio

Research output: Contribution to journalArticlepeer-review

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 languageEnglish
Pages (from-to)41-51
Number of pages11
JournalExtremophiles
Volume10
Issue number1
DOIs
Publication statusPublished - Feb 2006

Keywords

  • Cold adaptation
  • DsbA
  • Gene regulation
  • Protein folding
  • Pseudoalteromonas haloplanktis
  • Thiol disulfide oxidoreductase pathways

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Microbiology

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