Stress-Induced Protein S-Glutathionylation in Arabidopsis1 (Record no. 41399)

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control field MX-MdCICY
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control field 20250625124654.0
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Transcribing agency CICY
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Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) B-7065
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Title Stress-Induced Protein S-Glutathionylation in Arabidopsis1
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Volume/sequential designation Plant Physiology, 138, p.2233-2244, 2005
520 3# - SUMMARY, ETC.
Summary, etc. S-Glutathionylation (thiolation)is a ubiquitous redox-sensitive and reversible modification of protein cysteinyl residues that can directly regulate their activity. While well established in animals, little is known about the formation and function of these mixed disulfides in plants. After labeling the intracellular glutathione pool with [35S]cysteine, suspension cultures of Arabidopsis (Arabidopsis thaliana ecotype Columbia)were shown to undergo a large increase in protein thiolation following treatment with the oxidant ert-butylhydroperoxide. To identify proteins undergoing thiolation, a combination of in vivo and in vitro labeling methods utilizing biotinylated, oxidized glutathione (GSSG-biotin)was developed to isolate Arabidopsis proteins/protein complexes that can be reversibly glutathionylated. Following two-dimensional polyacrylamide gel electrophoresis and matrixassisted laser desorption/ionization time of flight mass spectrometry proteomics, a total of 79 polypeptides were identified, representing a mixture of proteins that underwent direct thiolation as well as proteins complexed with thiolated polypeptides. The mechanism of thiolation of five proteins, dehydroascorbate reductase (AtDHAR1), zeta-class glutathione transferase (AtGSTZ1), nitrilase (AtNit1), alcohol dehydrogenase (AtADH1), and methionine synthase (AtMetS), was studied using the respective purified recombinant proteins. AtDHAR1, AtGSTZ1, and to a lesser degree AtNit1 underwent spontaneous thiolation with GSSG-biotin through modification of active-site cysteines. The thiolation of AtADH1 and AtMetS required the presence of unidentified Arabidopsis proteins, with this activity being inhibited by S-modifying agents. The potential role of thiolation in regulating metabolism in Arabidopsis is discussed and compared with other known redox regulatory systems operating in plants.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Dixon, D.P.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Skipsey, M.
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Personal name Grundy, N.M.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Edwards, R.
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Uniform Resource Identifier <a href="https://drive.google.com/file/d/1gwUJIQHWgsr5YtBLoyVYHButHHwCzoNc/view?usp=drivesdk">https://drive.google.com/file/d/1gwUJIQHWgsr5YtBLoyVYHButHHwCzoNc/view?usp=drivesdk</a>
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Source of classification or shelving scheme Clasificación local
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  Clasificación local     Ref1 CICY CICY Documento préstamo interbibliotecario 25.06.2025   B-7065 25.06.2025 25.06.2025 Documentos solicitados