Redox signal integration: from stimulus to networks and genes

Dietz K-J (2008)
PHYSIOLOGIA PLANTARUM 133(3): 459-468.

Download
Es wurde kein Volltext hochgeladen. Nur Publikationsnachweis!
Zeitschriftenaufsatz | Veröffentlicht | Englisch
Abstract / Bemerkung
Recent research has established redox-dependent thiol modification of proteins as a major regulatory layer superimposed on most cell functional categories in plants. Modern proteomics and forward as well as reverse genetics approaches have enabled the identification of a high number of novel targets of redox regulation. Redox-controlled processes range from metabolism to transport, transcription and translation. Gene activity regulation by transcription factors such as TGA, Athb-9 and RAP2 directly or indirectly is controlled by the redox state. Knowledge on putative redox sensors such as the peroxiredoxins, on redox transmitters including thioredoxins and glutaredoxins and biochemical mechanisms of their linkage to the metabolic redox environment has emerged as the framework of a functional redox regulatory network. Its basic principle is similar in eukaryotic cells and particularly complex in the photosynthesizing chloroplast. Methods and knowledge are now at hand to develop a quantitative understanding of redox signalling and the redox regulatory network in the eukaryotic cell.
Erscheinungsjahr
Zeitschriftentitel
PHYSIOLOGIA PLANTARUM
Band
133
Zeitschriftennummer
3
Seite
459-468
ISSN
eISSN
PUB-ID

Zitieren

Dietz K-J. Redox signal integration: from stimulus to networks and genes. PHYSIOLOGIA PLANTARUM. 2008;133(3):459-468.
Dietz, K. - J. (2008). Redox signal integration: from stimulus to networks and genes. PHYSIOLOGIA PLANTARUM, 133(3), 459-468. doi:10.1111/j.1399-3054.2008.01120.x
Dietz, K. - J. (2008). Redox signal integration: from stimulus to networks and genes. PHYSIOLOGIA PLANTARUM 133, 459-468.
Dietz, K.-J., 2008. Redox signal integration: from stimulus to networks and genes. PHYSIOLOGIA PLANTARUM, 133(3), p 459-468.
K.-J. Dietz, “Redox signal integration: from stimulus to networks and genes”, PHYSIOLOGIA PLANTARUM, vol. 133, 2008, pp. 459-468.
Dietz, K.-J.: Redox signal integration: from stimulus to networks and genes. PHYSIOLOGIA PLANTARUM. 133, 459-468 (2008).
Dietz, Karl-Josef. “Redox signal integration: from stimulus to networks and genes”. PHYSIOLOGIA PLANTARUM 133.3 (2008): 459-468.

19 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

A noncanonical auxin-sensing mechanism is required for organ morphogenesis in Arabidopsis.
Simonini S, Deb J, Moubayidin L, Stephenson P, Valluru M, Freire-Rios A, Sorefan K, Weijers D, Friml J, Østergaard L., Genes Dev 30(20), 2016
PMID: 27898393
Early perturbation in mitochondria redox homeostasis in response to environmental stress predicts cell fate in diatoms.
van Creveld SG, Rosenwasser S, Schatz D, Koren I, Vardi A., ISME J 9(2), 2015
PMID: 25083933
The hydrogen peroxide-sensitive proteome of the chloroplast in vitro and in vivo.
Muthuramalingam M, Matros A, Scheibe R, Mock HP, Dietz KJ., Front Plant Sci 4(), 2013
PMID: 23516120
Mechanisms of nitrosylation and denitrosylation of cytoplasmic glyceraldehyde-3-phosphate dehydrogenase from Arabidopsis thaliana.
Zaffagnini M, Morisse S, Bedhomme M, Marchand CH, Festa M, Rouhier N, Lemaire SD, Trost P., J Biol Chem 288(31), 2013
PMID: 23749990
Role of CBFs as integrators of chloroplast redox, phytochrome and plant hormone signaling during cold acclimation.
Kurepin LV, Dahal KP, Savitch LV, Singh J, Bode R, Ivanov AG, Hurry V, Hüner NP., Int J Mol Sci 14(6), 2013
PMID: 23778089
The conformational bases for the two functionalities of 2-cysteine peroxiredoxins as peroxidase and chaperone.
König J, Galliardt H, Jütte P, Schäper S, Dittmann L, Dietz KJ., J Exp Bot 64(11), 2013
PMID: 23828546
Subset of heat-shock transcription factors required for the early response of Arabidopsis to excess light.
Jung HS, Crisp PA, Estavillo GM, Cole B, Hong F, Mockler TC, Pogson BJ, Chory J., Proc Natl Acad Sci U S A 110(35), 2013
PMID: 23918368
Hydrogen peroxide functions as a secondary messenger for brassinosteroids-induced CO2 assimilation and carbohydrate metabolism in Cucumis sativus.
Jiang YP, Cheng F, Zhou YH, Xia XJ, Mao WH, Shi K, Chen ZX, Yu JQ., J Zhejiang Univ Sci B 13(10), 2012
PMID: 23024048
Organelles contribute differentially to reactive oxygen species-related events during extended darkness.
Rosenwasser S, Rot I, Sollner E, Meyer AJ, Smith Y, Leviatan N, Fluhr R, Friedman H., Plant Physiol 156(1), 2011
PMID: 21372201
Peroxiredoxins in plants and cyanobacteria.
Dietz KJ., Antioxid Redox Signal 15(4), 2011
PMID: 21194355
Modulation of redox homeostasis under suboptimal conditions by Arabidopsis nudix hydrolase 7.
Jambunathan N, Penaganti A, Tang Y, Mahalingam R., BMC Plant Biol 10(), 2010
PMID: 20704736
Arabidopsis basic leucine-zipper transcription factors TGA9 and TGA10 interact with floral glutaredoxins ROXY1 and ROXY2 and are redundantly required for anther development.
Murmu J, Bush MJ, DeLong C, Li S, Xu M, Khan M, Malcolmson C, Fobert PR, Zachgo S, Hepworth SR., Plant Physiol 154(3), 2010
PMID: 20805327
A novel extended family of stromal thioredoxins.
Cain P, Hall M, Schröder WP, Kieselbach T, Robinson C., Plant Mol Biol 70(3), 2009
PMID: 19259774

70 References

Daten bereitgestellt von Europe PubMed Central.

Thioredoxins, glutaredoxins, and glutathionylation: new crosstalks to explore.
Michelet L, Zaffagnini M, Massot V, Keryer E, Vanacker H, Miginiac-Maslow M, Issakidis-Bourguet E, Lemaire SD., Photosyn. Res. 89(2-3), 2006
PMID: 17089213
The mitochondrial type II peroxiredoxin from poplar
Gama F, Keech O, Eymery F, Finkemeier I, Gelhaye E, Gardestrom P, Dietz KJ, Rey P, Jacquot JP, Rouhier N., Physiol Plant 129(1), 2007
PMID: IND43860515
Redox regulation and antioxidative defence in Arabidopsis leaves viewed from a systems biology perspective.
Wormuth D, Heiber I, Shaikali J, Kandlbinder A, Baier M, Dietz KJ., J. Biotechnol. 129(2), 2007
PMID: 17207878
Cross-talk between singlet oxygen- and hydrogen peroxide-dependent signaling of stress responses in Arabidopsis thaliana.
Laloi C, Stachowiak M, Pers-Kamczyc E, Warzych E, Murgia I, Apel K., Proc. Natl. Acad. Sci. U.S.A. 104(2), 2007
PMID: 17197417
Non-reductive modulation of chloroplast fructose-1,6-bisphosphatase by 2-Cys peroxiredoxin.
Caporaletti D, D'Alessio AC, Rodriguez-Suarez RJ, Senn AM, Duek PD, Wolosiuk RA., Biochem. Biophys. Res. Commun. 355(3), 2007
PMID: 17307139
Mitochondrial redox biology and homeostasis in plants.
Noctor G, De Paepe R, Foyer CH., Trends Plant Sci. 12(3), 2007
PMID: 17293156
SA-inducible Arabidopsis glutaredoxin interacts with TGA factors and suppresses JA-responsive PDF1.2 transcription.
Ndamukong I, Abdallat AA, Thurow C, Fode B, Zander M, Weigel R, Gatz C., Plant J. 50(1), 2007
PMID: 17397508
Crystal structures of a poplar thioredoxin peroxidase that exhibits the structure of glutathione peroxidases: insights into redox-driven conformational changes.
Koh CS, Didierjean C, Navrot N, Panjikar S, Mulliert G, Rouhier N, Jacquot JP, Aubry A, Shawkataly O, Corbier C., J. Mol. Biol. 370(3), 2007
PMID: 17531267
Functional, structural, and spectroscopic characterization of a glutathione-ligated [2Fe-2S] cluster in poplar glutaredoxin C1.
Rouhier N, Unno H, Bandyopadhyay S, Masip L, Kim SK, Hirasawa M, Gualberto JM, Lattard V, Kusunoki M, Knaff DB, Georgiou G, Hase T, Johnson MK, Jacquot JP., Proc. Natl. Acad. Sci. U.S.A. 104(18), 2007
PMID: 17460036
S-glutathionylation in protein redox regulation.
Dalle-Donne I, Rossi R, Giustarini D, Colombo R, Milzani A., Free Radic. Biol. Med. 43(6), 2007
PMID: 17697933
Redox-sensitive GFP in Arabidopsis thaliana is a quantitative biosensor for the redox potential of the cellular glutathione redox buffer.
Meyer AJ, Brach T, Marty L, Kreye S, Rouhier N, Jacquot JP, Hell R., Plant J. 52(5), 2007
PMID: 17892447
S-nitrosylation of peroxiredoxin II E promotes peroxynitrite-mediated tyrosine nitration.
Romero-Puertas MC, Laxa M, Matte A, Zaninotto F, Finkemeier I, Jones AM, Perazzolli M, Vandelle E, Dietz KJ, Delledonne M., Plant Cell 19(12), 2007
PMID: 18165327
TIC62 redox-regulated translocon composition and dynamics.
Stengel A, Benz P, Balsera M, Soll J, Bolter B., J. Biol. Chem. 283(11), 2008
PMID: 18180301
The redox-sensitive transcription factor Rap2.4a controls nuclear expression of 2-Cys peroxiredoxin A and other chloroplast antioxidant enzymes.
Shaikhali J, Heiber I, Seidel T, Stroher E, Hiltscher H, Birkmann S, Dietz KJ, Baier M., BMC Plant Biol. 8(), 2008
PMID: 18439303

Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®

Quellen

PMID: 18429942
PubMed | Europe PMC

Suchen in

Google Scholar