Universität Bielefeld Biochemie und Physiologie der Pflanzen Universität Bielefeld

Sitemap Help print version
Universität |  International |  Benutzer | 
 You are here:
 · Universität Bielefeld
   · Faculty of Biology
     · Bio4
 
 
.
· General information
· Coworkers
· Research
· Teaching
· Seminars
· Recent Papers and Reviews
· Contact

 
Peroxiredoxine

Peroxiredoxins


Peroxiredoxins are nuclear encoded thiol-proteins with molecular masses of 17 to 24 kDa. They are ubiquitious peroxidases reducing a broad spectrum of peroxides like H2O2, lipid hydroperoxide and peroxinitrite. In the genome of Arabidopsis thaliana 10 peroxiredoxins are encoded. Four of them are post-translationally targeted to the chlorolasts and one is imported into mitochondria. The others are cytosolic or localised in the nucleus (1-Cys Prx). Recent work supports more and more the hypothesis that peroxiredoxins are not only antioxidant proteins, but also involved in „redox signalling“. In our group a team of PhD students and post-docs works on the various aspects of peroxiredoxins ranging from
- analysis of the physiological function in antioxidant defense and "redox signalling"
- cell- tissue and stress-specificity of gene expression
- Redox regulation of promoter activity
- analysis of gene suppression, T-DNA-insertion and over-expression lines
- biochemical and physiological characterisation
- looking for interaction partners
Peroxiredoxins are being investigated in the model plant Arabidopsis thaliana, Brassica napus and the prokaryotic model organisms Synechocystis sp. PCC 6803.


Reviews:

Dietz K-J, Jacob S, Oelze ML, Laxa M, Tognetti V, de Miranda SM, Baier M, Finkemeier I (2006) The function of peroxiredoxins in plant organelle redoc metabolism. J. Exp. Bot. 57, 1697 - 1709

Dietz KJ, Stork T, Finkemeier I, Lamkemeyer P, Li WX, El-Tayeb MA, Michel KP, Pistorius E, Baier M (2004) The role of peroxiredoxins in oxygenic photosynthesis of cyanobacteria and higher plants: peroxide detoxification or redox sensing? In: Photoprotection, photoinhibition, gene regulation, and environment. Demmig-Adams B, Adams W, Mattoo A, eds. Kluwer Acad Press

Dietz KJ (2003) Plant peroxiredoxins. Annu. Rev. Plant Biol. 54, 93-107.

Dietz KJ, Horling F, Konig J and Baier M (2002) The function of the chloroplast 2-cysteine peroxiredoxin in peroxide detoxification and its regulation. J Exp Bot 53: 1321-1329

Baier M, Dietz K-J (1999) Alkyl hydroperoxide reductases: the way out of the oxidative breakdown of lipids in chloropasts. Trends in Plant Sci. 4, 166 -168


Orginalarbeiten:

Pena-Ahumada A, Kahmann U, Dietz K-J, Baier M (2006) Regulation of peroxiredoxin expression versus expression of Halliwell-Asada-Cycle enzymes during early seedling development in Arabidopsis thaliana. Photosynth. Res. (in press)

Groten K, Dutilleul C, van Heerden PDR, Vanacker N, Bernard S, Finkemeier I, Dietz KJ, Foyer CH (2006) Redox regulation of peroxiredoxin and proteinases by ascorbate and thiols during pea root nodule senescence. FEBS Lett. 580, 1269 - 1276

Lamkemeyer P, Laxa M, Collin V, Li W, Finkemeier I
, Schöttler MA, Holtkamp V, Tognetti VB, Issakidis-Bourguet E, Kandlbinder A, Weis E, Miginiac-Maslow M, Dietz K-J  (2006) Peroxiredoxin Q of Arabidopsis thaliana is attached to the thylakoids and functions in contrext of photosynthesis. Plant J. 45, 968 - 981

Stork T, Michel KP, Pistorius EK, Dietz K-J (2005) Bioinformatic analysis of the genomes of the cyanobacteria Synechocystis sp. PCC 6803 and Synechococcus elongatus PCC 7942 for the presence of peroxiredoxins and their transcript regulation under stress. J. Exp. Bot. 56, 3193 - 3206

Finkemeier I, Goodman M, Lamkemeyer P, Kandlbinder A, Sweetlove LJ, Dietz K-J (2005) The mitochondrial type II peroxiredoxin F is essential for redox homeostasis and root growth of Arabidopsis thaliana under stress. J. Biol. Chem. 280, 12168 - 12180

Baier M, Ströher E, Dietz K-J (2004) The acceptor availability at photosystem I and ABA control nuclear expression of 2-Cys peroxiredoxin-A in Arabidopsis thaliana. Plant Cell Physiol. 45, 997 - 1006

König J, Lotte K, Plessow R, Brockhinke A, Baier M, Dietz KJ (2003) Reaction mechanism of the 2-Cys peroxiredoxin: Role of the C-terminus and the quarternary structure. J. Biol. Chem. 278, 24409 - 24420

Horling F, Lamkemeyer P, König J, Finkemeier I, Baier M, Kandlbinder A, Dietz KJ (2003) Divergent light-, ascorbate- and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis thaliana. Plant Physiology, 131, 317-325.

Horling F, König J, Dietz KJ (2002) Type II peroxiredoxin C, a member of the peroxiredoxin family of Arabidopsis thaliana: its expression and activity in comparison with other peroxiredoxins. Plant Physiol. Biochem. 40 (6-8) 491-499

König J, Baier M, Horling F, Kahmann U, Harris G, Schürmann P, Dietz KJ (2002) The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox-hierarchy of photosynthetic electron flux. Proc. Natl. Acad. Sci. USA 99, 5738-5743

Baier M, König J, Horling F, Dietz KJ (2002) Detoxification of peroxides in the chloroplast: What's the role of 2-Cys peroxiredoxins. Proceedings of the International Congress on Photosynthesis, August 2001, Brisbaine, Australia S3-004

Dietz KJ, Horling F, König J, Baier M (2002) The function of the chloroplast 2-cysteine peroxiredoxin in peroxide detoxification and its regulation. J. Exp. Bot. 53 (372), 1321-1329

Horling F, Baier M, Dietz K-J (2001) The cellular redox poise regulates expression of the peroxide detoxifying chloroplast 2-Cys peroxiredoxin in the liverwort Riccia fluitans. Planta 214, 283-287

Baier M, Noctor G, Foyer CH, Dietz KJ (2000) Antisense suppression of 2-Cys peroxiredoxin in Arabidopsis thaliana specifically enhances the activities and expression of enzymes associated with ascorbate metabolism, but not glutathione metabolism. Plant Physiol. 124, 823-832

Baier M, Dietz K-J (1999) Protective function of chloroplast 2-Cys peroxiredoxin in photosynthesis: Evidence from transgenic Arabidopsis thaliana. Plant Physiol. 119, 1407 - 1414

Baier M, Dietz K-J (1999) The plant 2-Cys peroxiredoxin protects from oxidative damage in chloroplasts. In: Proceedings of the XI Int. Congr. on Photosynthesis, Garab et al. eds., Budapest. pp. 2003-2006

Yamamoto H, Miyake C, Dietz K-J, Tomizawa KI, Murata N, Yokota A (1999) Thioredoxin peroxidase in the cyanobacterium Synechocystis sp. PCC 6803. FEBS Letters 447, 269-273

Baier M, Dietz K-J (1998) The plant 2-Cys peroxiredoxin BAS1 is a homodimer whose subunits are linked by disulfide bonds and non-covalent interactions. In: Antioxidants in Higher Plants: Biosynthesis, Characteristics, Actions and Specific Functions in Stress Defence. Noga G., Schmitz M. eds., Shaker Verlag, Aachen. pp. 31-37

Klughammer B, Baier M, Dietz K-J (1998) Inactivation by gene disruption of 2-cysteine-peroxiredoxin in Synechocystis sp. PCC 6803 leads to increased stress sensitivity. Physiol. Plant., 104, 699 - 706

Baier, M, Dietz, K-J (1997) The plant 2-Cys peroxiredoxin BAS1 is a nuclear encoded chloroplast protein. Its expressional regulation, phylogenetic origin, and implications for its specific physiological function in plants. Plant J. 12, 179-190

Baier, M, Dietz, K-J (1996) The two-Cys peroxiredoxin Bas1: Insight in a new family of plant peroxidases. In: ‘Plant peroxidases, biochemistry and physiology’ Obinger, C., Burner, U., Ebermann, R., Penel, C., Greppin H. (eds.), University of Agriculture, Wien, Juni 1996, pp. 204-209

Baier, M, Dietz K-J (1996) 2-Cys peroxiredoxin bas 1 from Arabidopsis thaliana.Plant Physiol. - Plant Gene Register 111, 651

Baier, M, Dietz, K-J (1996) Primary structure and expression of plant homologues of animal and fungal thioredoxin-dependent peroxide reductases and bacterial alkyl hydroperoxide reductases. Plant Mol. Biol. 31, 553-564



For further information, please contact: Karl-Josef Dietz (e-mail) und Margarete Baier (e-mail)


 
To top of page Sitemap Help print version