Multiple Redox and Non-Redox Interactions Define 2-Cys Peroxiredoxin as a Regulatory Hub in the Chloroplast

Muthuramalingam M, Seidel T, Laxa M, de Miranda SMN, Gaertner F, Stroeher E, Kandlbinder A, Dietz K-J (2009)
MOLECULAR PLANT 2(6): 1273-1288.

Download
Es wurde kein Volltext hochgeladen. Nur Publikationsnachweis!
Zeitschriftenaufsatz | Veröffentlicht | Englisch
Autor
; ; ; ; ; ; ;
Abstract / Bemerkung
In plants, the highly abundant 2-cysteine peroxiredoxin (2-CysPrx) is associated with the chloroplast and involved in protecting photosynthesis. This work addresses the multiple interactions of the 2-CysPrx in the chloroplast, which depend on its redox state. Transcript co-regulation analysis showed a strong linkage to the peptidyl-prolyl-cis/trans isomerase Cyclophilin 20-3 (Cyp20-3) and other components of the photosynthetic apparatus. Co-expression in protoplasts and quantification of fluorescence resonance energy transfer (FRET) efficiency in vivo confirmed protein interactions of 2-CysPrx with Cyp20-3 as well as NADPH-dependent thioredoxin reductase C (NTRC), while thioredoxin x (Trx-x) did not form complexes that could enable FRET. Likewise, changes in FRET of fluorescently labeled 2-CysPrx in vitro and in vivo proved redox dependent dynamics of 2-CysPrx. Addition of Cyp20-3 to an in vitro peroxidase assay with 2-CysPrx had no significant effect on peroxide reduction. Also, in the presence of NTRC, addition of Cyp20-3 did not further enhance peroxide reduction. In addition, 2-CysPrx functioned as chaperone and inhibited aggregation of citrate synthase during heat treatment. This activity was partly inhibited by Cyp20-3. As a new interaction partner of decameric 2-CysPrx, photosystem II could be identified after chloroplast fractionation and in pull-down assays after reconstitution. In summary, the data indicate a dynamic function of plant 2-CysPrx as redox sensor, chaperone, and regulator in the chloroplast with diverse functions beyond its role as thiol peroxidase.
Erscheinungsjahr
Zeitschriftentitel
MOLECULAR PLANT
Band
2
Zeitschriftennummer
6
Seite
1273-1288
ISSN
eISSN
PUB-ID

Zitieren

Muthuramalingam M, Seidel T, Laxa M, et al. Multiple Redox and Non-Redox Interactions Define 2-Cys Peroxiredoxin as a Regulatory Hub in the Chloroplast. MOLECULAR PLANT. 2009;2(6):1273-1288.
Muthuramalingam, M., Seidel, T., Laxa, M., de Miranda, S. M. N., Gaertner, F., Stroeher, E., Kandlbinder, A., et al. (2009). Multiple Redox and Non-Redox Interactions Define 2-Cys Peroxiredoxin as a Regulatory Hub in the Chloroplast. MOLECULAR PLANT, 2(6), 1273-1288. doi:10.1093/mp/ssp089
Muthuramalingam, M., Seidel, T., Laxa, M., de Miranda, S. M. N., Gaertner, F., Stroeher, E., Kandlbinder, A., and Dietz, K. - J. (2009). Multiple Redox and Non-Redox Interactions Define 2-Cys Peroxiredoxin as a Regulatory Hub in the Chloroplast. MOLECULAR PLANT 2, 1273-1288.
Muthuramalingam, M., et al., 2009. Multiple Redox and Non-Redox Interactions Define 2-Cys Peroxiredoxin as a Regulatory Hub in the Chloroplast. MOLECULAR PLANT, 2(6), p 1273-1288.
M. Muthuramalingam, et al., “Multiple Redox and Non-Redox Interactions Define 2-Cys Peroxiredoxin as a Regulatory Hub in the Chloroplast”, MOLECULAR PLANT, vol. 2, 2009, pp. 1273-1288.
Muthuramalingam, M., Seidel, T., Laxa, M., de Miranda, S.M.N., Gaertner, F., Stroeher, E., Kandlbinder, A., Dietz, K.-J.: Multiple Redox and Non-Redox Interactions Define 2-Cys Peroxiredoxin as a Regulatory Hub in the Chloroplast. MOLECULAR PLANT. 2, 1273-1288 (2009).
Muthuramalingam, Meenakumari, Seidel, Thorsten, Laxa, Miriam, de Miranda, Susana M. Nunes, Gaertner, Florian, Stroeher, Elke, Kandlbinder, Andrea, and Dietz, Karl-Josef. “Multiple Redox and Non-Redox Interactions Define 2-Cys Peroxiredoxin as a Regulatory Hub in the Chloroplast”. MOLECULAR PLANT 2.6 (2009): 1273-1288.

42 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Kaede for detection of protein oligomerization.
Wolf H, Barisas BG, Dietz KJ, Seidel T., Mol Plant 6(5), 2013
PMID: 23430050
Protein disulfide isomerase 2 of Chlamydomonas reinhardtii is involved in circadian rhythm regulation.
Filonova A, Haemsch P, Gebauer C, Weisheit W, Wagner V., Mol Plant 6(5), 2013
PMID: 23475997
Cyclophilin 20-3 relays a 12-oxo-phytodienoic acid signal during stress responsive regulation of cellular redox homeostasis.
Park SW, Li W, Viehhauser A, He B, Kim S, Nilsson AK, Andersson MX, Kittle JD, Ambavaram MM, Luan S, Esker AR, Tholl D, Cimini D, Ellerström M, Coaker G, Mitchell TK, Pereira A, Dietz KJ, Lawrence CB., Proc Natl Acad Sci U S A 110(23), 2013
PMID: 23671085
The function of the NADPH thioredoxin reductase C-2-Cys peroxiredoxin system in plastid redox regulation and signalling.
Cejudo FJ, Ferrández J, Cano B, Puerto-Galán L, Guinea M., FEBS Lett 586(18), 2012
PMID: 22796111
Update on chloroplast research: new tools, new topics, and new trends.
Armbruster U, Pesaresi P, Pribil M, Hertle A, Leister D., Mol Plant 4(1), 2011
PMID: 20924030
ATP and Mg2+ promote the reversible oligomerization and aggregation of chloroplast 2-Cys peroxiredoxin.
Aran M, Ferrero D, Wolosiuk A, Mora-García S, Wolosiuk RA., J Biol Chem 286(26), 2011
PMID: 21525006
Peroxiredoxins in plants and cyanobacteria.
Dietz KJ., Antioxid Redox Signal 15(4), 2011
PMID: 21194355
Functional analysis of the pathways for 2-Cys peroxiredoxin reduction in Arabidopsis thaliana chloroplasts.
Pulido P, Spínola MC, Kirchsteiger K, Guinea M, Pascual MB, Sahrawy M, Sandalio LM, Dietz KJ, González M, Cejudo FJ., J Exp Bot 61(14), 2010
PMID: 20616155
Hubs and bottlenecks in plant molecular signalling networks.
Dietz KJ, Jacquot JP, Harris G., New Phytol 188(4), 2010
PMID: 20958306
Dynamic translocation of ligand-complexed DNA through solid-state nanopores with optical tweezers.
Sischka A, Spiering A, Khaksar M, Laxa M, König J, Dietz KJ, Anselmetti D., J Phys Condens Matter 22(45), 2010
PMID: 21339608

51 References

Daten bereitgestellt von Europe PubMed Central.

Thioredoxin peroxidase in the Cyanobacterium Synechocystis sp. PCC 6803.
Yamamoto H, Miyake C, Dietz KJ, Tomizawa K, Murata N, Yokota A., FEBS Lett. 447(2-3), 1999
PMID: 10214959

Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®

Quellen

PMID: 19995730
PubMed | Europe PMC

Suchen in

Google Scholar