Thioredoxin 2 from<i>Escherichia coli</i>is not involved<i>in vivo</i>in the recycling process of methionine sulfoxide reductase activities

Jacob, Christophe; Kriznik, Alexandre; Boschi‐Muller, Sandrine; Branlant, Guy

doi:10.1016/j.febslet.2011.04.070

Cited by 13 publications

(10 citation statements)

References 26 publications

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“…This system is ''leaky,'' and even under non-inducing conditions there is a basal expression level from the T7 promoter (see Experimental Procedures for details), which is sufficient to compensate the growth deficiency of the E. coli Trx À strain with the plasmid encoding for the gene of E. coli thioredoxin 1 (Figure 2A). This suggests that the basal expression level leads to thioredoxin concentrations within the complemented E. coli Trx À strain comparable to the normal thioredoxin concentration within E. coli ($10 2 mM) (Jacob et al, 2011).…”

Section: E Coli Strains Used In This Workmentioning

confidence: 87%

Using Resurrected Ancestral Proviral Proteins to Engineer Virus Resistance

et al. 2017

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Proviral factors are host proteins hijacked by viruses for processes essential for virus propagation such as cellular entry and replication. Pathogens and their hosts co-evolve. It follows that replacing a proviral factor with a functional ancestral form of the same protein could prevent viral propagation without fatally compromising organismal fitness. Here, we provide proof of concept of this notion. Thioredoxins serve as general oxidoreductases in all known cells. We report that several laboratory resurrections of Precambrian thioredoxins display substantial levels of functionality within Escherichia coli. Unlike E. coli thioredoxin, however, these ancestral thioredoxins are not efficiently recruited by the bacteriophage T7 for its replisome and therefore prevent phage propagation in E. coli. These results suggest an approach to the engineering of virus resistance. Diseases caused by viruses may have a devastating effect in agriculture. We discuss how the suggested approach could be applied to the engineering of plant virus resistance.

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Section: E Coli Strains Used In This Workmentioning

confidence: 87%

Using Resurrected Ancestral Proviral Proteins to Engineer Virus Resistance

et al. 2017

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“…To regain their reductase activity, MsrAs use reducing pathways (35), such as the Trx/TrxR pathway, which is used by most organisms to maintain a reducing environment within cells. Highlighting the importance of the Trx reducing pathway, Trx deletion mutants of Met auxotrophs of E. coli (36) and yeast (37) are incapable of using Met-SO as a Met source. In this study, we have shown that Cd-MsrA is also coupled to the Trx/ TrxR pathway, by monitoring NADPH consumption in a coupled enzyme assay.…”

Section: Discussionmentioning

confidence: 99%

Corynebacterium diphtheriae Methionine Sulfoxide Reductase A Exploits a Unique Mycothiol Redox Relay Mechanism

Tossounian

Pedre

Wahni

et al. 2015

Journal of Biological Chemistry

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Background: Methionine sulfoxide post-translational modifications have an important new signaling role in cells. Results: Methionine sulfoxide reductase MsrA of the pathogenic actinomycete Corynebacterium diphtheriae (Cd-MsrA) uses a unique intramolecular redox relay mechanism coupled to mycothiol. Conclusion: For methionine sulfoxide control, Cd-MsrA is flexible in receiving electrons from both the thioredoxin and the mycothiol pathways. Significance: C. diphtheriae MsrA is a redox regulator for methionine sulfoxide signaling.

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“…8B), further confirming that the Mrx1/Mtr/MSH system is not operative under normal conditions. In E. coli, the GSH/Grx/GR system cannot supply the Trx/TrxR system for the regeneration of the MsrA activity (53), as a Met-auxotrophic E. coli strain cannot grow in the presence of MetO when the genes coding for Trx1 and Trx2 are inactivated (24). However, it is technically difficult to investigate whether the Mrx1/Mtr/MSH system could supply the Trx/TrxR system, because the trx gene in C. glutamicum seems to be essential, and it cannot be deleted (20).…”

Section: Discussionmentioning

confidence: 99%

Corynebacterium glutamicum Methionine Sulfoxide Reductase A Uses both Mycoredoxin and Thioredoxin for Regeneration and Oxidative Stress Resistance

Zhang

Chaudhry

et al. 2015

Appl Environ Microbiol

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A erobic metabolism and oxidative stress lead to the production and accumulation of reactive oxygen species (ROS). ROS induce oxidative damage to macromolecules, such as proteins, lipids, and DNA, ultimately inducing cell death and disease. In proteins, oxidation modification occurs mainly at the sulfur-containing amino acids, such as cysteine (Cys) and methionine (Met) (1). Oxidation of methionine leads to the formation of the R and S diastereomers of methionine sulfoxide (MetO) and results in either conformational change or loss of function of proteins (2). However, this oxidation can be reversed by the action of methionine sulfoxide reductase (Msr), a ubiquitous monomeric enzyme that reduces both free and protein-bound MetO by employing sulfenic acid chemistry (3). Two structurally unrelated classes of Msrs, MsrAs and MsrBs, reduce the S and R MetO diastereoisomers, respectively. MsrA has been implicated in physiological processes, such as protection of cells against oxidative damage and extension of the life span, and acts as a virulence factor in some bacterial pathogens (4-6).MsrAs can be classified into three groups, 3-Cys, 2-Cys, and 1-Cys MsrAs, according to the number of redox-active Cys residues. Three-Cys MsrAs, such as the Escherichia coli and Bos taurus enzymes, have three Cys residues involved in catalysis, one of which functions as a catalytic residue and the other two as resolving residues (7,8). Two-Cys MsrAs, such as the Saccharomyces cerevisiae and Streptococcus pneumoniae enzymes, possess a single resolving Cys in addition to the catalytic Cys (4, 9). The 3-Cys and 2-Cys MsrAs present similar catalytic mechanisms. First, the catalytic Cys residue attacks a sulfoxide moiety of the substrate and then forms a sulfenic acid intermediate, with a concomitant release of Met as a product. Second, the sulfenic acid of the catalytic Cys forms an intramolecular disulfide bond with a resolving Cys. For 2-Cys MsrAs, this disulfide bond is directly reduced by a reducing agent to regenerate the active form of the enzyme, such as thioredoxin (Trx), which is a natural reducing agent for Msrs. For 3-Cys MsrAs, which perform an extra thiol-disulfide exchange reaction, the first disulfide bond is further reduced by the second

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Thioredoxin 2 fromEscherichia coliis not involvedin vivoin the recycling process of methionine sulfoxide reductase activities

Cited by 13 publications

References 26 publications

Using Resurrected Ancestral Proviral Proteins to Engineer Virus Resistance

Using Resurrected Ancestral Proviral Proteins to Engineer Virus Resistance

Corynebacterium diphtheriae Methionine Sulfoxide Reductase A Exploits a Unique Mycothiol Redox Relay Mechanism

Corynebacterium glutamicum Methionine Sulfoxide Reductase A Uses both Mycoredoxin and Thioredoxin for Regeneration and Oxidative Stress Resistance

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