| Diverse roles for chloroplast stromal and thylakoid-bound ascorbate peroxidases in plant stress responses. | |
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MedLine Citation:
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PMID: 18318659 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Photosynthetic light reactions comprise a significant source of hydrogen peroxide (H(2)O(2)) in illuminated leaves. APXs (ascorbate peroxidases) reduce H(2)O(2) to water and play an important role in the antioxidant system of plants. In the present study we addressed the significance of chloroplast APXs in stress tolerance and signalling in Arabidopsis thaliana. To this end, T-DNA (transfer DNA) insertion mutants tapx, sapx and tapx sapx, lacking the tAPX (thylakoid-bound APX), sAPX (stromal APX) or both respectively, were characterized. Photo-oxidative stress during germination led to bleaching of chloroplasts in sapx single-mutant and particularly in the tapx sapx double-mutant plants, whereas the greening process of wild-type and tapx plants was only partially impaired. Mature leaves of tapx sapx double mutants were also susceptible to short-term photo-oxidative stress induced by high light or methyl viologen treatments. After a 2-week acclimation period under high light or under low temperature, none of the mutants exhibited enhanced stress symptoms. Immunoblot analysis revealed that high-light-stress-acclimated tapx sapx double mutants compensated for the absence of tAPX and sAPX by increasing the level of 2-cysteine peroxiredoxin. Furthermore, the absence of tAPX and sAPX induced alterations in the transcriptomic profile of tapx sapx double-mutant plants already under quite optimal growth conditions. We conclude that sAPX is particularly important for photoprotection during the early greening process. In mature leaves, tAPX and sAPX are functionally redundant, and crucial upon sudden onset of oxidative stress. Moreover, chloroplast APXs contribute to chloroplast retrograde signalling pathways upon slight fluctuations in the accumulation of H(2)O(2) in chloroplasts. |
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Authors:
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Saijaliisa Kangasjärvi; Anna Lepistö; Kati Hännikäinen; Mirva Piippo; Eeva-Maria Luomala; Eva-Mari Aro; Eevi Rintamäki |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S. |
Journal Detail:
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Title: The Biochemical journal Volume: 412 ISSN: 1470-8728 ISO Abbreviation: Biochem. J. Publication Date: 2008 Jun |
Date Detail:
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Created Date: 2008-05-09 Completed Date: 2008-07-03 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 2984726R Medline TA: Biochem J Country: England |
Other Details:
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Languages: eng Pagination: 275-85 Citation Subset: IM |
Affiliation:
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Department of Biology, University of Turku, FI-20014 Turku, Finland. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Arabidopsis
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cytology*,
enzymology*,
genetics Arabidopsis Proteins / genetics, metabolism* Chloroplasts* / enzymology, ultrastructure Hydrogen Peroxide / metabolism Light Light-Harvesting Protein Complexes / chemistry, metabolism Mutation Oxidants / metabolism Oxidative Stress* Peroxidases / genetics, metabolism Peroxiredoxins / genetics, metabolism Phenotype Signal Transduction / physiology Thylakoids / enzymology* |
| Chemical | |
Reg. No./Substance:
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0/Arabidopsis Proteins; 0/Light-Harvesting Protein Complexes; 0/Oxidants; 7722-84-1/Hydrogen Peroxide; EC 1.11.1.-/Peroxidases; EC 1.11.1.11/ascorbate peroxidase; EC 1.11.1.15/Peroxiredoxins |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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