YajL, Prokaryotic Homolog of Parkinsonism-associated Protein DJ-1, Functions as a Covalent Chaperone for Thiol Proteome

Le, Hai Tuong; Gautier, Valérie; Kthiri, Fatoum; Malki, Abderrahim; Messaoudi, Nadia; Mihoub, Mouadh; Landoulsi, Ahmed; An, Young Jun; Shin, Sun Mi; Richarme, Gilbert

doi:10.1074/jbc.m111.299198

Cited by 38 publications

(60 citation statements)

References 49 publications

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“…The WT strain and the yajL mutant oxidized NADH at relative rates of 100 and 29, respectively, and deamino-NADH at relative rates of 41 and 5.3, respectively (Fig. 1d); thus NADH dehydrogenase I was almost inactive in the mutant (13 % of the parental strain activity, as reported previously; Le et al, 2012) [we also reported previously that the YajL-overproducing plasmid efficiently rescued (up to 86 %) the NADH dehydrogenase defect of the yajL mutant; Le et al, 2012)], whereas NADH dehydrogenase 2 was 41 % active. The weak global NADH dehydrogenase activity of the yajL mutant may be responsible for the high NADH/NAD ratio, fermentative metabolism and induction of alternative respiratory pathways (see below).…”

Section: Nadh Dehydrogenase Defectsupporting

confidence: 59%

“…Eukaryotic D-amino acid oxidases (which are restricted to D-amino acid detoxification) are of limited metabolic interest. Eukaryotic acyl-CoA dehydrogenases are involved in the first step of fatty acyl-CoA degradation and transfer hydrogens to quinones; however, the next oxidoreduction step of b-oxidation and acetyl-CoA oxidation in the Krebs cycle produce NADH, so they would be of little use to overcome NADH dehydrogenase defects (Abdallah et al, 2007;Bindoff et al, 1989;Calhoun & Gennis, 1993;Koebmann et al, 2002;Le et al, 2012;Schapira & Gegg, 2011). Proline oxidase catalyses the conversion of proline to D 1 -pyrroline-5-carboxylate and transfers hydrogens to quinones via FAD, whereas the reverse reaction, catalysed by D 1 -pyrroline-5-carboxylate reductase, uses NAD(P)H as a cofactor; consequently, both reactions produce a cycle of proline synthesis and degradation that can transfer redox potential between cellular compartments, and might contribute to bypassing NADH dehydrogenase 1 deficiency.…”

Section: Overexpression Of Alternative Respiratory Dehydrogenasesmentioning

confidence: 99%

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Fermentation and alternative respiration compensate for NADH dehydrogenase deficiency in a prokaryotic model of DJ-1-associated Parkinsonism

Messaoudi

Gautier²,

Dairou

et al. 2015

Microbiology

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YajL is the closest prokaryotic homologue of Parkinson's disease-associated DJ-1, a protein of undefined function involved in the oxidative stress response. We reported recently that YajL and DJ-1 protect cells against oxidative stress-induced protein aggregation by acting as covalent chaperones for the thiol proteome, including the NuoG subunit of NADH dehydrogenase 1, and that NADH dehydrogenase 1 activity is negligible in the yajL mutant. We report here that this mutant compensates for low NADH dehydrogenase activity by utilizing NADH-independent alternative dehydrogenases, including pyruvate oxidase PoxB and D-amino acid dehydrogenase DadA, and mixed acid aerobic fermentations characterized by acetate, lactate, succinate and ethanol excretion. The yajL mutant has a low adenylate energy charge favouring glycolytic flux, and a high NADH/NAD ratio favouring fermentations over pyruvate dehydrogenase and the Krebs cycle. DNA array analysis showed upregulation of genes involved in glycolytic and pentose phosphate pathways and alternative respiratory pathways. Moreover, the yajL mutant preferentially catabolized pyruvate-forming amino acids over Krebs cycle-related amino acids, and thus the yajL mutant utilizes pyruvate-centred respiro-fermentative metabolism to compensate for the NADH dehydrogenase 1 defect and constitutes an interesting model for studying eukaryotic respiratory complex I deficiencies, especially those associated with Alzheimer's and Parkinson's diseases.

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Section: Nadh Dehydrogenase Defectsupporting

confidence: 59%

Section: Overexpression Of Alternative Respiratory Dehydrogenasesmentioning

confidence: 99%

Fermentation and alternative respiration compensate for NADH dehydrogenase deficiency in a prokaryotic model of DJ-1-associated Parkinsonism

Messaoudi

Gautier²,

Dairou

et al. 2015

Microbiology

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“…YajL is an anti-oxidative-stress chaperone, which promotes disulfide formation to help maintain order in the thiol proteome (69). Interestingly, the human homolog of YajL, DJ-1, is also an antioxidative stress protein, and its mutations are known to cause familial Parkinsonism (70).…”

Section: Discussionmentioning

confidence: 99%

Identification of 2-oxohistidine Interacting Proteins Using E. coli Proteome Chips

Lin

Tsai

Liu

et al. 2016

Molecular & Cellular Proteomics

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Cellular proteins are constantly damaged by reactive oxygen species generated by cellular respiration. Because of its metal-chelating property, the histidine residue is easily oxidized in the presence of Cu/Fe ions and H 2 O 2 via metal-catalyzed oxidation, usually converted to 2-oxohistidine. We hypothesized that cells may have evolved antioxidant defenses against the generation of 2-oxohistidine residues on proteins, and therefore there would be cellular proteins which specifically interact with this oxidized side chain. Using two chemically synthesized peptide probes containing 2-oxohistidine, high-throughput interactome screening was conducted using the E. coli K12 proteome microarray containing >4200 proteins. Ten interacting proteins were identified, and successfully validated using a third peptide probe, fluorescence polarization assays, as well as binding constant measurements. We discovered that 9 out of 10 identified proteins seemed to be involved in redox-related cellular functions. We also built the functional interaction network to reveal their interacting proteins. The network showed that our interacting proteins were enriched in oxido-reduction processes, ion binding, and carbon metabolism. A consensus motif was identified among these 10 bacterial interacting proteins based on bioinformatic analysis, which also appeared to be present on human S100A1 protein. Besides, we found that the consensus binding motif among our identified proteins, including bacteria and human, were located within ␣-helices and faced the outside of proteins. The combination of chemically engineered peptide probes with proteome microarrays proves to be an efficient discovery platform for protein interactomes of unusual post-translational modifications, and sensitive enough to detect even the insertion of a single oxygen atom in this case.

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“…Also, several macromolecules that participate in translation have been found to be a target of oxidation in in vivo or in vitro experiments indicating that translation is directly targeted by oxidative species. In bacteria, these target macromolecules include elongation factors Tu [30][31][32][33][34], Ts (EF-Ts) [32] and G (EF-G) [8,9,22,32,35], several ribosomal proteins [31,36,37], tRNA [38][39][40][41][42] and aminoacyl-tRNA synthetases (aaRS) [31,34,36,37,43,44] (Table 1). rRNA and mRNA has also been shown to be oxidized in vivo in eukaryotes [19,25,26], but in bacteria this has not been tested.…”

Section: Oxidation Of the Translation Machinery During Oxidative Stressmentioning

confidence: 99%

Protein Synthesis and the Stress Response

Katz¹,

Orellana²

2012

Cell-Free Protein Synthesis

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YajL, Prokaryotic Homolog of Parkinsonism-associated Protein DJ-1, Functions as a Covalent Chaperone for Thiol Proteome

Cited by 38 publications

References 49 publications

Fermentation and alternative respiration compensate for NADH dehydrogenase deficiency in a prokaryotic model of DJ-1-associated Parkinsonism

Fermentation and alternative respiration compensate for NADH dehydrogenase deficiency in a prokaryotic model of DJ-1-associated Parkinsonism

Identification of 2-oxohistidine Interacting Proteins Using E. coli Proteome Chips

Protein Synthesis and the Stress Response

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