Peroxiredoxin Q of Arabidopsis thaliana is attached to the thylakoids and functions in context of photosynthesis

Lamkemeyer P, Laxa M, Collin V, Li W, Finkemeier I, Schottler MA, Holtkamp V, Tognetti VB, Issakidis-Bourguet E, Kandlbinder A, Weis E, et al. (2006)
PLANT JOURNAL 45(6): 968-981.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Abstract / Bemerkung
Peroxiredoxin Q (Prx Q) is one out of 10 peroxiredoxins encoded in the genome of Arabidopsis thaliana, and one out of four that are targeted to plastids. Peroxiredoxin Q functions as a monomeric protein and represents about 0.3% of chloroplast proteins. It attaches to the thylakoid membrane and is detected in preparations enriched in photosystem II complexes. Peroxiredoxin Q decomposes peroxides using thioredoxin as an electron donor with a substrate preference of H2O2 > cumene hydroperoxide >> butyl hydroperoxide >> linoleoyl hydroperoxide and insignificant affinity towards complex phospholipid hydroperoxide. Plants with decreased levels of Prx Q did not have an apparently different phenotype from wildtype at the plant level. However, similar to antisense 2-cysteine (2-Cys) Prx plants [Baier, M. et al. (2000) Plant Physiol., 124, 823-832], Prx Q-deficient plants had a decreased sensitivity to oxidants in a leaf slice test as indicated by chlorophyll a fluorescence measurements. Increased fluorescence ratios of photosystem II to I at 77 K and modified transcript levels of plastid- and nuclear-encoded proteins show that regulatory mechanisms are at work to compensate for the lack of Prx Q. Apparently Prx Q attaches to photosystem II and has a specific function distinct from 2-Cys peroxiredoxin in protecting photosynthesis. Its absence causes metabolic changes that are sensed and trigger appropriate compensatory responses.
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Zeitschriftentitel
PLANT JOURNAL
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45
Zeitschriftennummer
6
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968-981
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Lamkemeyer P, Laxa M, Collin V, et al. Peroxiredoxin Q of Arabidopsis thaliana is attached to the thylakoids and functions in context of photosynthesis. PLANT JOURNAL. 2006;45(6):968-981.
Lamkemeyer, P., Laxa, M., Collin, V., Li, W., Finkemeier, I., Schottler, M. A., Holtkamp, V., et al. (2006). Peroxiredoxin Q of Arabidopsis thaliana is attached to the thylakoids and functions in context of photosynthesis. PLANT JOURNAL, 45(6), 968-981. doi:10.1111/j.1365-313X.2006.02665.x
Lamkemeyer, P., Laxa, M., Collin, V., Li, W., Finkemeier, I., Schottler, M. A., Holtkamp, V., Tognetti, V. B., Issakidis-Bourguet, E., Kandlbinder, A., et al. (2006). Peroxiredoxin Q of Arabidopsis thaliana is attached to the thylakoids and functions in context of photosynthesis. PLANT JOURNAL 45, 968-981.
Lamkemeyer, P., et al., 2006. Peroxiredoxin Q of Arabidopsis thaliana is attached to the thylakoids and functions in context of photosynthesis. PLANT JOURNAL, 45(6), p 968-981.
P. Lamkemeyer, et al., “Peroxiredoxin Q of Arabidopsis thaliana is attached to the thylakoids and functions in context of photosynthesis”, PLANT JOURNAL, vol. 45, 2006, pp. 968-981.
Lamkemeyer, P., Laxa, M., Collin, V., Li, W., Finkemeier, I., Schottler, M.A., Holtkamp, V., Tognetti, V.B., Issakidis-Bourguet, E., Kandlbinder, A., Weis, E., Miginiac-Maslow, M., Dietz, K.-J.: Peroxiredoxin Q of Arabidopsis thaliana is attached to the thylakoids and functions in context of photosynthesis. PLANT JOURNAL. 45, 968-981 (2006).
Lamkemeyer, P, Laxa, M, Collin, V, Li, W, Finkemeier, I, Schottler, MA, Holtkamp, V, Tognetti, VB, Issakidis-Bourguet, E, Kandlbinder, Andrea, Weis, E, Miginiac-Maslow, M, and Dietz, Karl-Josef. “Peroxiredoxin Q of Arabidopsis thaliana is attached to the thylakoids and functions in context of photosynthesis”. PLANT JOURNAL 45.6 (2006): 968-981.

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Glutaredoxins and thioredoxins in plants.
Meyer Y, Siala W, Bashandy T, Riondet C, Vignols F, Reichheld JP., Biochim Biophys Acta 1783(4), 2008
PMID: 18047840
The peroxiredoxin and glutathione peroxidase families in Chlamydomonas reinhardtii.
Dayer R, Fischer BB, Eggen RI, Lemaire SD., Genetics 179(1), 2008
PMID: 18493039
The ferredoxin/thioredoxin system of oxygenic photosynthesis.
Schürmann P, Buchanan BB., Antioxid Redox Signal 10(7), 2008
PMID: 18377232
Functional analysis and expression characteristics of chloroplastic Prx IIE.
Gama F, Bréhélin C, Gelhaye E, Meyer Y, Jacquot JP, Rey P, Rouhier N., Physiol Plant 133(3), 2008
PMID: 18422870
Redox signal integration: from stimulus to networks and genes.
Dietz KJ., Physiol Plant 133(3), 2008
PMID: 18429942
Functional analysis and expression characteristics of chloroplastic Prx IIE
Gama F, Bréhélin C, Gelhaye E, Meyer Y, Jacquot JP, Rey P, Rouhier N., Physiol Plant 133(3), 2008
PMID: IND44069763
Hexameric oligomerization of mitochondrial peroxiredoxin PrxIIF and formation of an ultrahigh affinity complex with its electron donor thioredoxin Trx-o.
Barranco-Medina S, Krell T, Bernier-Villamor L, Sevilla F, Lázaro JJ, Dietz KJ., J Exp Bot 59(12), 2008
PMID: 18632730
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
The Arabidopsis thaliana sulfiredoxin is a plastidic cysteine-sulfinic acid reductase involved in the photooxidative stress response.
Rey P, Bécuwe N, Barrault MB, Rumeau D, Havaux M, Biteau B, Toledano MB., Plant J 49(3), 2007
PMID: 17217469
The mitochondrial type II peroxiredoxin from poplar
Gama F, Keech O, Eymery F, Finkemeier I, Gelhaye E, Gardeström P, Dietz KJ, Rey P, Jacquot JP, Rouhier N., Physiol Plant 129(1), 2007
PMID: IND43860515
Thioredoxins in chloroplasts.
Lemaire SD, Michelet L, Zaffagnini M, Massot V, Issakidis-Bourguet E., Curr Genet 51(6), 2007
PMID: 17431629
Plant thioredoxins are key actors in the oxidative stress response.
Vieira Dos Santos C, Rey P., Trends Plant Sci 11(7), 2006
PMID: 16782394
The Prx Q protein of Arabidopsis thaliana is a member of the luminal chloroplast proteome.
Petersson UA, Kieselbach T, García-Cerdán JG, Schröder WP., FEBS Lett 580(26), 2006
PMID: 17054949

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