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

Baier M, Dietz K-J (1997)
The Plant Journal 12(1): 179-190.

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2-Cys peroxiredoxins constitute a family of enzymes which catalyze the transfer of electrons from sulfhydryl residues to peroxides and are ubiquitously distributed among all organisms. This paper characterizes the higher plant 2-Cysperoxiredoxin BAS1. (i) Escherichia coil over-expressing BAS1 exhibit increased tolerance for alkyl hydroperoxides in vivo. This result substantiates the peroxiredoxin function of BAS1. (ii) BAS1 protein is associated with the soluble chloroplast fraction of mesophyll protoplasts. Import and processing of in vitro-transcribed and cell-free translated BAS1 protein into isolated chloroplasts provides conclusive evidence that the plant-specific N-terminal extension of bas1 encodes the chloroplast import signal which targets the pre-form of BAS1 to the chloroplast stroma where it is cleaved to its mature size. (iii) Genomic analysis reveals that the targeting signal is encoded by a separate exon in Arabidopsis thaliana. (iv) The amino acid sequence of the BAS1 core protein of higher plants has a higher degree of similarity to open reading frames in the genome of the bluegreen algae Synechochystis PCC sp. 6803 and in the plastome of the red algae Porphyra purpurea than to any other nuclear-encoded P-Cys peroxiredoxin. Therefore, it is tempting to speculate that the chloroplast import signal was added to an ancestor gene of endosymbiotic origin in the course of plant evolution. (v) The bas1 gene expression is regulated under the control of the cellular redox state which is in accordance with the anti-oxidant function of the enzyme. While oxidative stressors increased expression only slightly, antioxidants such as reduced thiols strongly suppressed the transcript level. The implications of these findings are discussed with respect to the possible physiological functions of BAS1.
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Baier M, Dietz K-J. 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. The Plant Journal. 1997;12(1):179-190.
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. The Plant Journal, 12(1), 179-190. doi:10.1046/j.1365-313X.1997.12010179.x
Baier, M., and 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. The Plant Journal 12, 179-190.
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. The Plant Journal, 12(1), p 179-190.
M. Baier and K.-J. Dietz, “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”, The Plant Journal, vol. 12, 1997, pp. 179-190.
Baier, M., Dietz, K.-J.: 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. The Plant Journal. 12, 179-190 (1997).
Baier, Margarete, and Dietz, Karl-Josef. “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”. The Plant Journal 12.1 (1997): 179-190.
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93 Citations in Europe PMC

Data provided by Europe PubMed Central.

Plant peroxiredoxins.
Dietz KJ., Annu Rev Plant Biol 54(), 2003
PMID: 14502986
Redox signaling in the chloroplast: the ferredoxin/thioredoxin system.
Schürmann P., Antioxid Redox Signal 5(1), 2003
PMID: 12626118
Isolation and characterization of a thioredoxin-dependent peroxidase from Chlamydomonas reinhardtii.
Goyer A, Haslekås C, Miginiac-Maslow M, Klein U, Le Marechal P, Jacquot JP, Decottignies P., Eur J Biochem 269(1), 2002
PMID: 11784321
Peroxiredoxins.
Hofmann B, Hecht HJ, Flohé L., Biol Chem 383(3-4), 2002
PMID: 12033427
The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox-hierarchy of photosynthetic electron flux.
König J, Baier M, Horling F, Kahmann U, Harris G, Schürmann P, Dietz KJ., Proc Natl Acad Sci U S A 99(8), 2002
PMID: 11929977
A method for detection of overoxidation of cysteines: peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stress.
Wagner E, Luche S, Penna L, Chevallet M, Van Dorsselaer A, Leize-Wagner E, Rabilloud T., Biochem J 366(pt 3), 2002
PMID: 12059788
The impact of oxidative stress on Arabidopsis mitochondria.
Sweetlove LJ, Heazlewood JL, Herald V, Holtzapffel R, Day DA, Leaver CJ, Millar AH., Plant J 32(6), 2002
PMID: 12492832
Comprehensive survey of proteins targeted by chloroplast thioredoxin.
Motohashi K, Kondoh A, Stumpp MT, Hisabori T., Proc Natl Acad Sci U S A 98(20), 2001
PMID: 11553771
Peroxide processing in photosynthesis: antioxidant coupling and redox signalling.
Noctor G, Veljovic-Jovanovic S, Foyer CH., Philos Trans R Soc Lond B Biol Sci 355(1402), 2000
PMID: 11128000
Rice 1Cys-peroxiredoxin over-expressed in transgenic tobacco does not maintain dormancy but enhances antioxidant activity.
Lee KO, Jang HH, Jung BG, Chi YH, Lee JY, Choi YO, Lee JR, Lim CO, Cho MJ, Lee SY., FEBS Lett 486(2), 2000
PMID: 11113447
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
In vivo role of catalase-peroxidase in synechocystis sp. strain PCC 6803.
Tichy M, Vermaas W., J Bacteriol 181(6), 1999
PMID: 10074082
Cloning and expression of a new isotype of the peroxiredoxin gene of Chinese cabbage and its comparison to 2Cys-peroxiredoxin isolated from the same plant.
Choi YO, Cheong NE, Lee KO, Jung BG, Hong CH, Jeong JH, Chi YH, Kim K, Cho MJ, Lee SY., Biochem Biophys Res Commun 258(3), 1999
PMID: 10329461

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