MDR quinone oxidoreductases: The human and yeast ζ-crystallins

Porté, Sergio; Crosas, Eva; Yakovtseva, Evgenia A.; Biosca, Josep A.; Farrés, Jaume; Fernández, María Rosario Salinas; Parés, Xavier

doi:10.1016/j.cbi.2008.10.018

Cited by 19 publications

(27 citation statements)

References 30 publications

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“…The metabolic activity of guinea pig z-crystallin catalyzes quinone reductions via a single-electron reducing mechanism. The z-crystallin reaction produces a radical semiquinone that generates reactive oxygen species (ROS) under aerobic conditions (Rao et al, 1992;Porté et al, 2009). In plants, the best characterized z-crystallin is P1-ZCr (also known as AT-AER arkenal reductase or NADPH:2-alkenal a,bhydrogenase) encoded by the Arabidopsis AT5G16990 locus.…”

Section: Discussionmentioning

confidence: 99%

A Single-Electron Reducing Quinone Oxidoreductase Is Necessary to Induce Haustorium Development in the Root Parasitic Plant Triphysaria

et al. 2010

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Parasitic plants in the Orobanchaceae develop haustoria in response to contact with host roots or chemical haustoriainducing factors. Experiments in this manuscript test the hypothesis that quinolic-inducing factors activate haustorium development via a signal mechanism initiated by redox cycling between quinone and hydroquinone states. Two cDNAs were previously isolated from roots of the parasitic plant Triphysaria versicolor that encode distinct quinone oxidoreductases. QR1 encodes a single-electron reducing NADPH quinone oxidoreductase similar to z-crystallin. The QR2 enzyme catalyzes two electron reductions typical of xenobiotic detoxification. QR1 and QR2 transcripts are upregulated in a primary response to chemical-inducing factors, but only QR1 was upregulated in response to host roots. RNA interference technology was used to reduce QR1 and QR2 transcripts in Triphysaria roots that were evaluated for their ability to form haustoria. There was a significant decrease in haustorium development in roots silenced for QR1 but not in roots silenced for QR2. The infrequent QR1 transgenic roots that did develop haustoria had levels of QR1 similar to those of nontransgenic roots. These experiments implicate QR1 as one of the earliest genes on the haustorium signal transduction pathway, encoding a quinone oxidoreductase necessary for the redox bioactivation of haustorial inducing factors.

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Section: Discussionmentioning

confidence: 99%

A Single-Electron Reducing Quinone Oxidoreductase Is Necessary to Induce Haustorium Development in the Root Parasitic Plant Triphysaria

et al. 2010

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“…The homolog of f-crystallin in Saccharomyces cerevisiae is Zta1, and it localizes in both the cytoplasm and the nucleus (Porte et al, 2009a). Zta1 is reported to have a similar substrate specificity to human (Fernandez et al, 2007) and guinea pig f-crystallins (Rao et al, 1992).…”

Section: Introductionmentioning

confidence: 98%

“…Cellular accumulation of quinones leads to serious cytotoxic effects in various ways (Bolton et al, 2000). Quinone dehydrogenase/oxidoreductases protect cells from the cytotoxic effects of quinones (Dinkova-Kostova and Talalay, 2000;Nioi and Hayes, 2004;Porte et al, 2009a). These enzymes catalyze the reduction of quinone to its corresponding hydroquinone, which is readily conjugated to either glucuronic acid or sulfate for excretion (Monks and Jones, 2002;Prestera et al, 1993).…”

Section: Introductionmentioning

confidence: 98%

“…NADPH-dependent quinone oxidoreductases (QORs, EC 1.6.5.5) belong to the nonmetallic reductase subfamily of the medium-chain dehydrogenase/reductase superfamily, which contains enzymes widespread in bacteria and eukaryotes (Porte et al, 2009a). The soluble QORs are distinct from the membrane-bound ones which are NADH-dependent, and contain noncovalently bound FMN and iron-sulfur clusters as prosthetic groups (Yagi, 1991).…”

Section: Introductionmentioning

confidence: 99%

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Structural insights into the cofactor-assisted substrate recognition of yeast quinone oxidoreductase Zta1

Guo¹,

Ma²,

Bao³

et al. 2011

Journal of Structural Biology

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“…Evidence also indicates a well-conserved catalytic role of f-crystallin. Thus, when sequences of three evolutionarily related structures, f-crystallin, yeast Zta1p and E. coli QOR, are compared, the substrate-binding pocket is significantly conserved, with much higher sequence identity (40%) than that of other parts of the molecule, including the cofactor-binding site (28%) [45]. Interestingly, all members of the f-crystallin subfamily exhibit a Tyr residue at each of the two positions homologous to Tyr53 and Tyr59, and their three-dimensional localization in the E. coli QOR structure [9] is identical to that in f-crystallin.…”

Section: Discussionmentioning

confidence: 99%

Kinetic and structural evidence of the alkenal/one reductase specificity of human ζ-crystallin

Porté

Reche

Shafqat

et al. 2010

Cell. Mol. Life Sci.

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Human ζ-crystallin is a Zn(2+)-lacking medium-chain dehydrogenase/reductase (MDR) included in the quinone oxidoreductase (QOR) family because of its activity with quinones. In the present work a novel enzymatic activity was characterized: the double bond α,β-hydrogenation of medium-chain 2-alkenals and 3-alkenones. The enzyme is especially active with lipid peroxidation products such as 4-hydroxyhexenal, and a role in their detoxification is discussed. This specificity is novel in the QOR family, and it is similar to that described in the distantly related alkenal/one reductase family. Moreover, we report the X-ray structure of ζ-crystallin, which represents the first structure solved for a tetrameric Zn(2+)-lacking MDR, and which allowed the identification of the active-site lining residues. Docking simulations suggest a role for Tyr53 and Tyr59 in catalysis. The kinetics of Tyr53Phe and Tyr59Phe mutants support the implication of Tyr53 in binding/catalysis of alkenal/one substrates, while Tyr59 is involved in the recognition of 4-OH-alkenals.

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MDR quinone oxidoreductases: The human and yeast ζ-crystallins

Cited by 19 publications

References 30 publications

A Single-Electron Reducing Quinone Oxidoreductase Is Necessary to Induce Haustorium Development in the Root Parasitic Plant Triphysaria

A Single-Electron Reducing Quinone Oxidoreductase Is Necessary to Induce Haustorium Development in the Root Parasitic Plant Triphysaria

Structural insights into the cofactor-assisted substrate recognition of yeast quinone oxidoreductase Zta1

Kinetic and structural evidence of the alkenal/one reductase specificity of human ζ-crystallin

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