Abstract
Methionine sulfoxide reductases (MSRA1 and MSRB) are proteins overproduced in Staphylococcus aureus during exposure with cell wall-active antibiotics. Later studies identified the presence of two additional MSRA proteins (MSRA2 and MSRA3) in S. aureus. These MSR proteins have been characterized in many other bacteria as well. This review provides the current knowledge about the conditions and regulatory network that mimic the expression of these MSR encoding genes and their role in defense from oxidative stress and virulence.
Highlights
Methionine sulfoxide reductases (MSRA1 and MSRB) are proteins overproduced in Staphylococcus aureus during exposure with cell wall-active antibiotics
Induction of the MSRA1/MSRB locus by cell wall-active antibiotics was inhibited by glycerol monolaurate that interfered with signal transduction pathways
When the percentage of oxidized methionine residues increased from exposure to 150 μM hypochlorous acid (HOCl), the cellular methionine sulfoxide (MetO) content increased from 6% to 22%, resulting in a 55% decrease in viability [47]
Summary
The presence of reactive oxygen species (ROS) is potentially damaging to all cellular macromolecules. Oxidizing agents, such as hydrogen peroxide (H2 O2 ), superoxides, and hydroxyl radicals, oxidize the sulfur atom of methionine residues, resulting in methionine sulfoxide (MetO). In 1981, an enzyme capable of reducing protein-bound methionine sulfoxide was identified [3,4]. These oxidized MetO residues are reduced back to methionine by methionine sulfoxide reductase (MSR) enzymes that restore normal protein functions [5,6]. The MetO/Met, MSRA/B-mediated oxidation and reduction of methionine residues are an important antioxidant mechanism [11], and methionine is no longer needed just for protein initiation [12]
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