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Thiol-Disulfide Exchange in Gram-Positive Firmicutes.
Davey, Lauren; Halperin, Scott A; Lee, Song F.
Affiliation
  • Davey L; Department of Microbiology and Immunology, Dalhousie University, Halifax, NS, B3H 1X5 Canada; Canadian Center for Vaccinology, Dalhousie University and the IWK Health Centre, Halifax, NS, B3K 6R8 Canada.
  • Halperin SA; Department of Microbiology and Immunology, Dalhousie University, Halifax, NS, B3H 1X5 Canada; Canadian Center for Vaccinology, Dalhousie University and the IWK Health Centre, Halifax, NS, B3K 6R8 Canada; Department of Pediatrics, Faculty of Medicine, Dalhousie University and the IWK Health Centre, Halifax, NS, B3K 6R8 Canada.
  • Lee SF; Department of Microbiology and Immunology, Dalhousie University, Halifax, NS, B3H 1X5 Canada; Canadian Center for Vaccinology, Dalhousie University and the IWK Health Centre, Halifax, NS, B3K 6R8 Canada; Department of Pediatrics, Faculty of Medicine, Dalhousie University and the IWK Health Centre, Halifax, NS, B3K 6R8 Canada; Department of Applied Oral Sciences, Faculty of Dentistry, Dalhousie University, Halifax, NS, B3H 4R2 Canada. Electronic address: Song.Lee@dal.ca.
Trends Microbiol ; 24(11): 902-915, 2016 11.
Article in En | MEDLINE | ID: mdl-27426970
ABSTRACT
Extracytoplasmic thiol-disulfide oxidoreductases (TDORs) catalyze the oxidation, reduction, and isomerization of protein disulfide bonds. Although these processes have been characterized in Gram-negative bacteria, the majority of Gram-positive TDORs have only recently been discovered. Results from recent studies have revealed distinct trends in the types of TDOR used by different groups of Gram-positive bacteria, and in their biological functions. Actinobacteria TDORs can be essential for viability, while Firmicute TDORs influence various physiological processes, including protein stability, oxidative stress resistance, bacteriocin production, and virulence. In this review we discuss the diverse extracytoplasmic TDORs used by Gram-positive bacteria, with a focus on Gram-positive Firmicutes.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Protein Disulfide Reductase (Glutathione) / Firmicutes Language: En Journal: Trends Microbiol Journal subject: MICROBIOLOGIA Year: 2016 Document type: Article

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Protein Disulfide Reductase (Glutathione) / Firmicutes Language: En Journal: Trends Microbiol Journal subject: MICROBIOLOGIA Year: 2016 Document type: Article