Oxidative stress, protein damage and repair in bacteria

Abstract

Oxidative damage can have a devastating effect on the structure and activity of proteins, and may even lead to cell death. The sulfur-containing amino acids cysteine and methionine are particularly susceptible to reactive oxygen species (ROS) and reactive chlorine species (RCS), which can damage proteins. In this Review, we discuss our current understanding of the reducing systems that enable bacteria to repair oxidatively damaged cysteine and methionine residues in the cytoplasm and in the bacterial cell envelope. We highlight the importance of these repair systems in bacterial physiology and virulence, and we discuss several examples of proteins that become activated by oxidation and help bacteria to respond to oxidative stress.

SdrA, an NADP(H)‐regenerating enzyme, is crucial for Coxiella burnetii to resist oxidative stress and replicate intracellularly

“…E. coli mutants that lack Trxs can still survive oxidative stress due to the presence of Grxs (Ezraty et al, ). Grxs also facilitate the reduction of oxidised cysteines in proteins damaged by oxidative stress.…”

“…Exposure to oxidative stress can damage DNA, membranes and proteins, and most organisms have therefore evolved a number of mechanisms to protect against the deleterious effects of oxidative stress (Ezraty, Gennaris, Barras, & Collet, 2017). The defence mechanisms utilised by C. burnetii are only partly characterised and are predominantly inferred from genome annotation (Mertens & Samuel, 2012).…”

“…E. coli mutants that lack Trxs can still survive oxidative stress due to the presence of Grxs (Ezraty et al, 2017). Grxs also facilitate the F I G U R E 6 Metabolites that are significantly different (p < .05, Benjamini-Hochberg-adjusted t test) in abundance between C. burnetii NMII and sdrA::Tn (a) and between the complemented sdrA mutant and sdrA:Tn (b) in the GC/MS steady state analysis.…”

Manganese‐Coordinated Tyrosine Bio Materials for the Sensing of Reactive Oxygen Species

“…Although ROS are involved in regulating signal transduction pathways, stimulating growth factor, and generating inflammatory response, their ability to modify biomolecules is a worrisome concern. Hence, it is desirable to detect the presence of ROS inside living cells before they can interfere with the structures and functions of biomolecules to create pathological conditions …”

“…Hence, it is desirable to detect the presence of ROS inside living cells before they can interfere with the structures and functions of biomolecules to create pathological conditions. [22][23][24] To recognise a ROS inside living cells, it is imperative to design biocompatible sensor materials that are stable and dynamic in nature. Although several metal-coordinated organic porous polymers were identified as efficient materials for sensing, [25,26] catalysis, [27] energy storage, [28] optoelectronic applications, [29] drug delivery, [30] these materials are not attractive for in vivo applications because of their bio-incompatibility and rigidity.…”