The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
Stress-Induced Protein S-Glutathionylation in Arabidopsis
Open accessAbstract
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 tert-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 matrix-assisted 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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Schafer, F. Q., & Buettner, G. R. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00480-4 · Cited by 4,587
Structure, mechanism and regulation of peroxiredoxins
Wood, Z. A., Schröder, E., Robin Harris, J., & Poole, L. B. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)00003-8 · Cited by 2,544
REDOX REGULATION: A Broadening Horizon
Buchanan, B. B., & Balmer, Y. (2005) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.56.032604.144246 · Cited by 885
Regulation of protein function by S‐glutathiolation in response to oxidative and nitrosative stress
Klatt, P., & Lamas, S. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01601.x · Cited by 745
Proteomic Identification of S -Nitrosylated Proteins in Arabidopsis
Lindermayr, C., Saalbach, G., & Durner, J. (2005) · Plant Physiology · doi:10.1104/pp.104.058719 · Cited by 734
Kliebenstein, D. J., Monde, R.-A., & Last, R. L. (1998) · Plant Physiology · doi:10.1104/pp.118.2.637 · Cited by 630
Fratelli, M., Demol, H., Puype, M., Casagrande, S., Eberini, I., Salmona, M., Bonetto, V., Mengozzi, M., Duffieux, F., Miclet, E., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.052592699 · Cited by 556
Functional Divergence in the Glutathione Transferase Superfamily in Plants
Dixon, D. P., Davis, B. G., & Edwards, R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202919200 · Cited by 428
Self-citationOxidative Stimulation of Glutathione Synthesis in Arabidopsis thaliana Suspension Cultures
May, M. J., & Leaver, C. J. (1993) · Plant Physiology · doi:10.1104/pp.103.2.621 · Cited by 427
Proteomics gives insight into the regulatory function of chloroplast thioredoxins
Balmer, Y., Koller, A., del Val, G., Manieri, W., Schürmann, P., & Buchanan, B. B. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.232703799 · Cited by 410
Comprehensive survey of proteins targeted by chloroplast thioredoxin
Motohashi, K., Kondoh, A., Stumpp, M. T., & Hisabori, T. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.191282098 · Cited by 390
The nitrilase superfamily: classification, structure and function.
Pace, H. C., & Brenner, C. (2001) · Genome biology · doi:10.1186/gb-2001-2-1-reviews0001 · Cited by 389
Thioredoxin links redox to the regulation of fundamental processes of plant mitochondria
Balmer, Y., Vensel, W. H., Tanaka, C. K., Hurkman, W. J., Gelhaye, E., Rouhier, N., Jacquot, J.-P., Manieri, W., Schürmann, P., Droux, M., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308583101 · Cited by 328
SHENTON, D., & GRANT, C. M. (2003) · Biochemical Journal · doi:10.1042/bj20030414 · Cited by 326
Lacombe, E., Hawkins, S., Van Doorsselaere, J., Piquemal, J., Goffner, D., Poeydomenge, O., Boudet, A., & Grima‐Pettenati, J. (1997) · The Plant Journal · doi:10.1046/j.1365-313x.1997.11030429.x · Cited by 324
Sulfenic Acid Formation in Human Serum Albumin by Hydrogen Peroxide and Peroxynitrite
Carballal, S., Radi, R., Kirk, M. C., Barnes, S., Freeman, B. A., & Alvarez, B. (2003) · Biochemistry · doi:10.1021/bi027434m · Cited by 313
Protein Thiol Modifications Visualized In Vivo
Leichert, L. I., & Jakob, U. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020333 · Cited by 228
Target Proteins of the Cytosolic Thioredoxins in Arabidopsis thaliana
Yamazaki, D., Motohashi, K., Kasama, T., Hara, Y., & Hisabori, T. (2004) · Plant and Cell Physiology · doi:10.1093/pcp/pch019 · Cited by 205
New targets of Arabidopsis thioredoxins revealed by proteomic analysis
Marchand, C., Le Maréchal, P., Meyer, Y., Miginiac‐Maslow, M., Issakidis‐Bourguet, E., & Decottignies, P. (2004) · PROTEOMICS · doi:10.1002/pmic.200400805 · Cited by 198
Structure of a Tau Class Glutathione S-Transferase from Wheat Active in Herbicide Detoxification,
Thom, R., Cummins, I., Dixon, D. P., Edwards, R., Cole, D. J., & Lapthorn, A. J. (2002) · Biochemistry · doi:10.1021/bi015964x · Cited by 176
Self-citationOxidative Stress Inactivates Cobalamin-Independent Methionine Synthase (MetE) in Escherichia coli
Hondorp, E. R., & Matthews, R. G. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020336 · Cited by 152
Thom, R., Dixon, D. P., Edwards, R., Cole, D. J., & Lapthorn, A. J. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4638 · Cited by 137
Self-citationDemasi, M., Silva, G. M., & Netto, L. E. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m209282200 · Cited by 126
Baty, J. W., Hampton, M. B., & Winterbourn, C. C. (2002) · PROTEOMICS · doi:10.1002/1615-9861(200209)2:9<1261::aid-prot1261>3.0.co;2-q · Cited by 125
Role of Protein -SH Groups in Redox Homeostasis— The Erythrocyte as a Model System
Simplicio, P. D., Cacace, M. G., Lusini, L., Giannerini, F., Giustarini, D., & Rossi, R. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.0694 · Cited by 123
Lind, C., Gerdes, R. G., Schuppe‐Koistinen, I., & Cotgreave, I. A. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8695 · Cited by 116
Thiol Oxidase Activity of Copper,Zinc Superoxide Dismutase
Winterbourn, C. C., Peskin, A. V., & Parsons-Mair, H. N. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107256200 · Cited by 101
Prade, L., Huber, R., & Bieseler, B. (1998) · Structure · doi:10.1016/s0969-2126(98)00143-9 · Cited by 88
Glutathiolation of the Proteasome Is Enhanced by Proteolytic Inhibitors
Demasi, M., Shringarpure, R., & Davies, K. J. A. (2001) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2332 · Cited by 87
Dixon, D. P., Cole, D. J., & Edwards, R. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.2125 · Cited by 85
Self-citationRedox proteomics: identification and functional role of glutathionylated proteins
Fratelli, M., Gianazza, E., & Ghezzi, P. (2004) · Expert Review of Proteomics · doi:10.1586/14789450.1.3.365 · Cited by 83
Defining the plant disulfide proteome
Lee, K., Lee, J., Kim, Y., Bae, D., Kang, K. Y., Yoon, S. C., & Lim, D. (2004) · Electrophoresis · doi:10.1002/elps.200305677 · Cited by 81
Cloning and characterization of the gene encoding IMP dehydrogenase from Arabidopsis thaliana
Collart, F., Osipiuk, J., Trent, J. D., Olsen, G. J., & Huberman, E. (1996) · Gene · doi:10.1016/0378-1119(96)00045-5 · Cited by 14
Cited by
Rouhier, N., Lemaire, S. D., & Jacquot, J.-P. (2008) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.59.032607.092811 · Cited by 573
Lillig, C. H., Berndt, C., & Holmgren, A. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.06.003 · Cited by 561
Houben, M., & Van de Poel, B. (2019) · Frontiers in Plant Science · doi:10.3389/fpls.2019.00695 · Cited by 420
Glutathione as an Antioxidant and Regulatory Molecule in Plants Under Abiotic Stress Conditions
Szalai, G., Kellős, T., Galiba, G., & Kocsy, G. (2009) · Journal of Plant Growth Regulation · doi:10.1007/s00344-008-9075-2 · Cited by 414
The regulation of ethylene biosynthesis: a complex multilevel control circuitry
Pattyn, J., Vaughan‐Hirsch, J., & Van de Poel, B. (2021) · New Phytologist · doi:10.1111/nph.16873 · Cited by 398
Metadata
- Authors
- Dixon, D. P., Skipsey, M., Grundy, N. M., & Edwards, R.
- Venue
- Plant Physiology
- Publisher
- Oxford University Press (OUP)
- Published
- 2005-07-29
- Volume
- 138
- Issue
- 4
- Pages
- 2233-2244
- ISSN
- 0032-0889 (ISSN-L)
- 1532-2548
- OpenAlex
- W2149495661
- Cited by
- 313
- References
- 33
- FWCI
- 5.53
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
