Disulfide Bond Formation in the Bacterial Periplasm: Major Achievements and Challenges Ahead

Denoncin, Katleen; Collet, Jean-François

doi:10.1089/ars.2012.4864

Cited by 110 publications

(103 citation statements)

References 50 publications

(55 reference statements)

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“…Electron-carriers (TC class 5) that transfer electrons from one side of the membrane to the other, thereby influencing cellular energetics [31], do not vary in numbers appreciably between the eight strains.…”

Section: Resultsmentioning

confidence: 99%

Transport proteins promoting Escherichia coli pathogenesis

Tang

Saier

2014

Microbial Pathogenesis

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Escherichia coli is a genetically diverse species infecting hundreds of millions of people worldwide annually. We examined seven well-characterized E. coli pathogens causing urinary tract infections, gastroenteritis, pyelonephritis and haemorrhagic colitis. Their transport proteins were identified and compared with each other and a non-pathogenic E. coli K12 strain to identify transport proteins related to pathogenesis. Each pathogen possesses a unique set of protein secretion systems for export to the cell surface or for injecting effector proteins into host cells. Pathogens have increased numbers of iron siderophore receptors and ABC iron uptake transporters, but the numbers and types of low-affinity secondary iron carriers were uniform in all strains. The presence of outer membrane iron complex receptors and high-affinity ABC iron uptake systems correlated, suggesting co-evolution. Each pathovar encodes a different set of pore-forming toxins and virulence-related outer membrane proteins lacking in K12. Intracellular pathogens proved to have a characteristically distinctive set of nutrient uptake porters, different from those of extracellular pathogens. The results presented in this report provide information about transport systems relevant to various types of E. coli pathogenesis that can be exploited in future basic and applied studies.

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Section: Resultsmentioning

confidence: 99%

Transport proteins promoting Escherichia coli pathogenesis

Tang

Saier

2014

Microbial Pathogenesis

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“…Here, we use a set of in silico approaches to systematically address the impact of disulfide bonds in these DRD features and experimentally validate theoretical predictions on selected DRD models. Oxidative folding catalysis occurs almost exclusively in the endoplasmic reticulum (ER), in the intermembrane space of mitochondria (41) in eukaryotes, and in the periplasm in bacteria (36). Systematic studies of DRDs folding rates in vivo are missing, mainly because disulfide bond formation occurs during translation and translocation, making the process complex to analyze.…”

Section: Discussionmentioning

confidence: 99%

Association Between Foldability and Aggregation Propensity in Small Disulfide-Rich Proteins

Fraga

Graña-Montes²,

Illa³

et al. 2014

Antioxidants & Redox Signaling

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Aims: Disulfide-rich domains (DRDs) are small proteins whose native structure is stabilized by the presence of covalent disulfide bonds. These domains are versatile and can perform a wide range of functions. Many of these domains readily unfold on disulfide bond reduction, suggesting that in the absence of covalent bonding they might display significant disorder. Results: Here, we analyzed the degree of disorder in 97 domains representative of the different DRDs families and demonstrate that, in terms of sequence, many of them can be classified as intrinsically disordered proteins (IDPs) or contain predicted disordered regions. The analysis of the aggregation propensity of these domains indicates that, similar to IDPs, their sequences are more soluble and have less aggregating regions than those of other globular domains, suggesting that they might have evolved to avoid aggregation after protein synthesis and before they can attain its compact and covalently linked native structure. Innovation and Conclusion: DRDs, which resemble IDPs in the reduced state and become globular when their disulfide bonds are formed, illustrate the link between protein folding and aggregation propensities and how these two properties cannot be easily dissociated, determining the main traits of the folding routes followed by these small proteins to attain their native oxidized states. Antioxid. Redox Signal. 21, 368-383.

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“…536 Gram-negative bacteria use thioredoxin-like enzymes to ensure the correct disulfide oxidation state during protein folding. 537 Similarly, disulfide moieties in secondary metabolites are essential in conferring biological activity through the generation of reactive oxygen species and by inactivating protein targets via covalent adduct formation (Scheme 53). The biosyntheses of three disulfide bond containing natural products, gliotoxin ( 231 ) 538,539 , holomycin ( 232 ) 540 , and romidepsin (233) 541 have been well-studied (Figure 25), and the enzymes involved in S–S bond formation are discussed below.…”

Section: S–s S–o and S–n Bond Forming Enzymesmentioning

confidence: 99%

Heteroatom–Heteroatom Bond Formation in Natural Product Biosynthesis

et al. 2017

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Natural products that contain functional groups with heteroatom-heteroatom linkages (X–X, where X = N, O, S, and P) are a small yet intriguing group of metabolites. The reactivity and diversity of these structural motifs has captured the interest of synthetic and biological chemists alike. Functional groups containing X–X bonds are found in all major classes of natural products and often impart significant biological activity. This review presents our current understanding of the biosynthetic logic and enzymatic chemistry involved in the construction of X–X bond containing functional groups within natural products. Elucidating and characterizing biosynthetic pathways that generate X–X bonds could both provide tools for biocatalysis and synthetic biology, as well as guide efforts to uncover new natural products containing these structural features.

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Disulfide Bond Formation in the Bacterial Periplasm: Major Achievements and Challenges Ahead

Cited by 110 publications

References 50 publications

Transport proteins promoting Escherichia coli pathogenesis

Transport proteins promoting Escherichia coli pathogenesis

Association Between Foldability and Aggregation Propensity in Small Disulfide-Rich Proteins

Heteroatom–Heteroatom Bond Formation in Natural Product Biosynthesis

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