NDLI: Expression of the Cyanidioschyzon merolae stromal ascorbate peroxidase in Arabidopsis thaliana enhances thermotolerance

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Expression of the Cyanidioschyzon merolae stromal ascorbate peroxidase in Arabidopsis thaliana enhances thermotolerance

Content Provider	Springer Nature Link
Author	Hirooka, Shunsuke Misumi, Osami Yoshida, Masaki Mori, Toshiyuki Nishida, Keiji Yagisawa, Fumi Yoshida, Yamato Fujiwara, Takayuki Kuroiwa, Haruko Kuroiwa, Tsuneyoshi
Copyright Year	2009
Abstract	The ability of the primitive red alga Cyanidioschyzon merolae to adapt to high temperatures was utilized to produce thermotolerant transgenic plants. C. merolae inhabits an extreme environment (42°C, pH 2.5) and the nuclear, mitochondrial, and plastid genomes have been sequenced. We analyzed expressed sequence tag (EST) data to reveal mechanisms of tolerance to high temperatures. The stromal ascorbate peroxidase (CmstAPX) that scavenges reactive oxygen species (ROS) was expressed at high levels (4th of 4,479 entries), thus, it offers clues to understanding high-temperature tolerance. CmstAPX has a chloroplast transit peptide (cTP) and a peroxidase domain. The peroxidase domain of CmstAPX has deletions and insertions when compared with that of Arabidopsis thaliana stromal APX (AtstAPX). To clarify aspects of tolerance to oxidative and high-temperature stress, we produced transgenic A. thaliana plants overexpressing CmstAPX and AtstAPX. CmstAPX plants showed higher activities of soluble APX than those of wild-type and AtstAPX plants. Fluorescence signals of a GFP fusion protein, immuno-fluorescence, and immunogold electron microscopy showed that CmstAPX was localized in the stroma of chloroplasts. Compared with wild-type plants and AtstAPX plants, CmstAPX plants were more tolerant to oxidative stress induced by methylviologen (MV, 0.4 μM) and high-temperature stress (33°C). CmstAPX plants retained the highest chlorophyll content when treated with MV and high temperature, and their stroma and chloroplasts remained intact in their chloroplasts, whereas they disintegrated in wild-type plants. Our results suggest that the increased activity of APX in the chloroplasts of CmstAPX plants increased thermotolerance by increasing ROS-scavenging capacity at high temperatures.
Starting Page	1881
Ending Page	1893
Page Count	13
File Format	PDF
ISSN	07217714
Journal	Plant Cell Reports
Volume Number	28
Issue Number	12
e-ISSN	1432203X
Language	English
Publisher	Springer-Verlag
Publisher Date	2009-10-27
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	High-temperature stress Ascorbate peroxidase Thermoacidic alga Transgenic plants Chloroplast structure Reactive oxygen species Plant Biochemistry Biotechnology Plant Sciences Cell Biology
Content Type	Text
Resource Type	Article
Subject	Plant Science Medicine Agronomy and Crop Science

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