Primary structure and expression of plant homologues of animal and fungal thioredoxin-dependent peroxide reductases and bacterial alkyl hydroperoxide reductases Authors
Received: 05 March 1996 Accepted: 08 March 1996 DOI:
Cite this article as: Baier, M. & Dietz, K. Plant Mol Biol (1996) 31: 553. doi:10.1007/BF00042228 Abstract
Higher plants express genes encoding peroxiredoxins of the two-cysteine type. This is concluded from the isolation of cDNAs from spinach (
Spinacia oleracea) and barley ( Hordeum vulgare cv. Gerbel) which are homologous to animal, fungal, and bacterial two-cysteine peroxiredoxins. Northern blot analysis indicated the presence of at least one corresponding gene in all angiosperms analyzed suggesting that bas1 is a member of an ubiquitous gene family encoding a protein of fundamental importance in oxidative stress defense also in plants. In barley, expression increased upon application of methyl viologen but was not affected by ozone. mRNA levels increased during deetiolation in the light. Maximal abundance of bas1 transcripts was observed in young developing shoot segments where cell division and elongation take place. Expression was insignificant in roots. The amount of bas1 protein was high in the leaf blade, particularly in etiolated plants, and did not respond to oxidative stress. bas1 protein was not detected in roots. From our data, we suggest that bas1 is an antioxidant enzyme particularly important in the developing shoot and photosynthesizing leaf. Key words cDNA-cloning expression Hordeum vulgare leaf peroxiredoxin shoot development Spinacia oleracea Abbreviations AhpC
C22 subunit of the alkyl hydroperoxide reductase
expressed sequence tag
thioredoxin-dependent peroxide reductase
CuZn superoxide dismutase
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