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Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
Published on: March 24, 2012
Thiol-Disulfide Exchange in Gram-Positive Firmicutes
Lauren Davey1, Scott A Halperin2, Song F Lee3
1Department 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.
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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