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Physiological and molecular changes in Oryza meridionalis Ng., a heat-tolerant species of wild rice
Oryza meridionalis Ng. is a wild relative of Oryza sativa L. found throughout northern Australia where temperatures regularly exceed 35 °C in the monsoon growing season. Heat tolerance in O. meridionalis was established by comparing leaf elongation and photosynthetic rates at 45 °C with plants maint...
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Formato: | Texto |
Lenguaje: | English |
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Oxford University Press
2010
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2791120/ https://www.ncbi.nlm.nih.gov/pubmed/19819927 http://dx.doi.org/10.1093/jxb/erp294 |
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author | Scafaro, Andrew P. Haynes, Paul A. Atwell, Brian J. |
author_facet | Scafaro, Andrew P. Haynes, Paul A. Atwell, Brian J. |
author_sort | Scafaro, Andrew P. |
collection | PubMed |
description | Oryza meridionalis Ng. is a wild relative of Oryza sativa L. found throughout northern Australia where temperatures regularly exceed 35 °C in the monsoon growing season. Heat tolerance in O. meridionalis was established by comparing leaf elongation and photosynthetic rates at 45 °C with plants maintained at 27 °C. By comparison with O. sativa ssp. japonica cv. Amaroo, O. meridionalis was heat tolerant. Elongation rates of the third leaf of O. meridionalis declined by 47% over 24 h at 45 °C compared with a 91% decrease for O. sativa. Net photosynthesis was significantly higher in O. sativa at 27 °C whereas the two species had the same assimilation rates at 45 °C. The leaf proteome and expression levels of individual heat-responsive genes provided insight into the heat response of O. meridionalis. After 24 h of heat exposure, many enzymes involved in the Calvin Cycle were more abundant, while mRNA of their genes generally decreased. Ferredoxin-NADP(H) oxidoreductase, a key enzyme in photosynthetic electron transport had both reduced abundance and gene expression, suggesting light reactions were highly susceptible to heat stress. Rubisco activase was strongly up-regulated after 24 h of heat, with the large isoform having the largest relative increase in protein abundance and a significant increase in gene expression. The protective proteins Cpn60, Hsp90, and Hsp70 all increased in both protein abundance and gene expression. A thiamine biosynthesis protein (THI1), previously shown to act protectively against stress, increased in abundance during heat, even as thiamine levels fell in O. meridionalis. |
format | Text |
id | pubmed-2791120 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-27911202009-12-10 Physiological and molecular changes in Oryza meridionalis Ng., a heat-tolerant species of wild rice Scafaro, Andrew P. Haynes, Paul A. Atwell, Brian J. J Exp Bot Research Papers Oryza meridionalis Ng. is a wild relative of Oryza sativa L. found throughout northern Australia where temperatures regularly exceed 35 °C in the monsoon growing season. Heat tolerance in O. meridionalis was established by comparing leaf elongation and photosynthetic rates at 45 °C with plants maintained at 27 °C. By comparison with O. sativa ssp. japonica cv. Amaroo, O. meridionalis was heat tolerant. Elongation rates of the third leaf of O. meridionalis declined by 47% over 24 h at 45 °C compared with a 91% decrease for O. sativa. Net photosynthesis was significantly higher in O. sativa at 27 °C whereas the two species had the same assimilation rates at 45 °C. The leaf proteome and expression levels of individual heat-responsive genes provided insight into the heat response of O. meridionalis. After 24 h of heat exposure, many enzymes involved in the Calvin Cycle were more abundant, while mRNA of their genes generally decreased. Ferredoxin-NADP(H) oxidoreductase, a key enzyme in photosynthetic electron transport had both reduced abundance and gene expression, suggesting light reactions were highly susceptible to heat stress. Rubisco activase was strongly up-regulated after 24 h of heat, with the large isoform having the largest relative increase in protein abundance and a significant increase in gene expression. The protective proteins Cpn60, Hsp90, and Hsp70 all increased in both protein abundance and gene expression. A thiamine biosynthesis protein (THI1), previously shown to act protectively against stress, increased in abundance during heat, even as thiamine levels fell in O. meridionalis. Oxford University Press 2010-01 2009-10-09 /pmc/articles/PMC2791120/ /pubmed/19819927 http://dx.doi.org/10.1093/jxb/erp294 Text en © 2009 The Author(s). This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details) |
spellingShingle | Research Papers Scafaro, Andrew P. Haynes, Paul A. Atwell, Brian J. Physiological and molecular changes in Oryza meridionalis Ng., a heat-tolerant species of wild rice |
title | Physiological and molecular changes in Oryza meridionalis Ng., a heat-tolerant species of wild rice |
title_full | Physiological and molecular changes in Oryza meridionalis Ng., a heat-tolerant species of wild rice |
title_fullStr | Physiological and molecular changes in Oryza meridionalis Ng., a heat-tolerant species of wild rice |
title_full_unstemmed | Physiological and molecular changes in Oryza meridionalis Ng., a heat-tolerant species of wild rice |
title_short | Physiological and molecular changes in Oryza meridionalis Ng., a heat-tolerant species of wild rice |
title_sort | physiological and molecular changes in oryza meridionalis ng., a heat-tolerant species of wild rice |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2791120/ https://www.ncbi.nlm.nih.gov/pubmed/19819927 http://dx.doi.org/10.1093/jxb/erp294 |
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