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Titolo:
Regulation of the plant-type 5 '-adenylyl sulfate reductase by oxidative stress
Autore:
Bick, JA; Setterdahl, AT; Knaff, DB; Chen, YC; Pitcher, LH; Zilinskas, BA; Leustek, T;
Indirizzi:
Rutgers State Univ, Ctr Agr Biotechnol, New Brunswick, NJ 08901 USA Rutgers State Univ New Brunswick NJ USA 08901 New Brunswick, NJ 08901 USA Rutgers State Univ, Environm & Plant Sci Dept, New Brunswick, NJ 08901 USARutgers State Univ New Brunswick NJ USA 08901 New Brunswick, NJ 08901 USA Texas Tech Univ, Dept Chem & Biochem, Lubbock, TX 79409 USA Texas Tech Univ Lubbock TX USA 79409 hem & Biochem, Lubbock, TX 79409 USA Texas Tech Univ, Ctr Biotechnol & Genom, Lubbock, TX 79409 USA Texas Tech Univ Lubbock TX USA 79409 chnol & Genom, Lubbock, TX 79409 USA
Titolo Testata:
BIOCHEMISTRY
fascicolo: 30, volume: 40, anno: 2001,
pagine: 9040 - 9048
SICI:
0006-2960(20010731)40:30<9040:ROTP5'>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
ADENOSINE 5'-PHOSPHOSULFATE SULFOTRANSFERASE; ESCHERICHIA-COLI CYTOPLASM; DISULFIDE BOND FORMATION; MOLECULAR-WEIGHT THIOLS; HORDEUM-VULGARE-L; ARABIDOPSIS-THALIANA; GLUTATHIONE SYNTHESIS; SUPEROXIDE-DISMUTASE; SULFUR ASSIMILATION; DEFICIENT MUTANT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Leustek, T Rutgers State Univ, Ctr Agr Biotechnol, 59 Dudley Rd, New Brunswick, NJ 08901 USA Rutgers State Univ 59 Dudley Rd New Brunswick NJ USA 08901 USA
Citazione:
J.A. Bick et al., "Regulation of the plant-type 5 '-adenylyl sulfate reductase by oxidative stress", BIOCHEM, 40(30), 2001, pp. 9040-9048

Abstract

5'-Adenylyl sulfate (APS) reductase (EC 1.8.4.9) catalyzes a key reaction in the plant sulfate assimilation pathway leading to the synthesis of cysteine and the antioxidant glutathione. In Arabidopsis thaliana APS reductase is encoded by a family of three genes. In vitro biochemical studies revealed that the enzyme product derived from one of them (APR1) is activated by oxidation, probably through the formation of a disulfide bond. The APR1 enzyme is 45-fold more active when expressed in a trxB strain of Escherichia coli than in a trxB(+) wild type. The enzyme is inactivated in vitro by treatment with disulfide reductants and is reactivated with thiol oxidants. Redox titrations show that the regulation site has a midpoint potential of -330mV at pH 8.5 and involves a two-electron redox reaction. Exposure of a variety of plants to ozone induces a rapid increase in APS reductase activity that correlates with the oxidation of the glutathione pool and is followed by an increase in free cysteine and total glutathione. During the response to ozone. the level of immunodetectable APS reductase enzyme does not increase. Treatment of A. thaliana seedlings with oxidized glutathione or paraquat induces APS reductase activity even when transcription or translation isblocked with inhibitors. The results suggest that a posttranslational mechanism controls APS reductase. A model is proposed whereby redox regulation of APS reductase provides a rapidly responding, self-regulating mechanism to control the glutathione synthesis necessary to combat oxidative stress.

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Documento generato il 29/11/20 alle ore 00:23:10