| Light intensity-dependent modulation of chlorophyll b biosynthesis and photosynthesis by overexpression of chlorophyllide a oxygenase in tobacco. | |
MedLine Citation:
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PMID: 22419827 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Chlorophyll b is synthesized by the oxidation of a methyl group on the B ring of a tetrapyrrole molecule to a formyl group by chlorophyllide a oxygenase (CAO). The full-length CAO from Arabidopsis (Arabidopsis thaliana) was overexpressed in tobacco (Nicotiana tabacum) that grows well at light intensities much higher than those tolerated by Arabidopsis. This resulted in an increased synthesis of glutamate semialdehyde, 5-aminolevulinic acid, magnesium-porphyrins, and chlorophylls. Overexpression of CAO resulted in increased chlorophyll b synthesis and a decreased chlorophyll a/b ratio in low light-grown as well as high light-grown tobacco plants; this effect, however, was more pronounced in high light. The increased potential of the protochlorophyllide oxidoreductase activity and chlorophyll biosynthesis compensated for the usual loss of chlorophylls in high light. Increased chlorophyll b synthesis in CAO-overexpressed plants was accompanied not only by an increased abundance of light-harvesting chlorophyll proteins but also of other proteins of the electron transport chain, which led to an increase in the capture of light as well as enhanced (40%-80%) electron transport rates of photosystems I and II at both limiting and saturating light intensities. Although the quantum yield of carbon dioxide fixation remained unchanged, the light-saturated photosynthetic carbon assimilation, starch content, and dry matter accumulation increased in CAO-overexpressed plants grown in both low- and high-light regimes. These results demonstrate that controlled up-regulation of chlorophyll b biosynthesis comodulates the expression of several thylakoid membrane proteins that increase both the antenna size and the electron transport rates and enhance carbon dioxide assimilation, starch content, and dry matter accumulation. |
Authors:
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Ajaya K Biswal; Gopal K Pattanayak; Shiv S Pandey; Sadhu Leelavathi; Vanga S Reddy; Govindjee; Baishnab C Tripathy |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2012-03-14 |
Journal Detail:
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Title: Plant physiology Volume: 159 ISSN: 1532-2548 ISO Abbreviation: Plant Physiol. Publication Date: 2012 May |
Date Detail:
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Created Date: 2012-05-04 Completed Date: 2012-08-23 Revised Date: 2013-06-26 |
Medline Journal Info:
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Nlm Unique ID: 0401224 Medline TA: Plant Physiol Country: United States |
Other Details:
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Languages: eng Pagination: 433-49 Citation Subset: IM |
Affiliation:
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School of Life Sciences, Jawaharlal Nehru University, New Delhi 110067, India. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Aminolevulinic Acid
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metabolism Arabidopsis / genetics, metabolism Carbon Dioxide / metabolism Chlorophyll / biosynthesis* Electron Transport Enzyme Activation Gene Expression Regulation, Plant Genes, Plant Light* Oxygenases / genetics, metabolism* Phenotype Photosynthesis* Photosystem I Protein Complex / genetics, metabolism Photosystem II Protein Complex / genetics, metabolism Plant Leaves / enzymology, genetics, radiation effects Plant Proteins / genetics, metabolism Plants, Genetically Modified / enzymology, genetics, radiation effects Starch / metabolism Thylakoid Membrane Proteins / genetics, metabolism Tobacco / enzymology*, genetics, radiation effects Transgenes |
| Chemical | |
Reg. No./Substance:
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0/Photosystem I Protein Complex; 0/Photosystem II Protein Complex; 0/Plant Proteins; 0/Thylakoid Membrane Proteins; 106-60-5/Aminolevulinic Acid; 124-38-9/Carbon Dioxide; 1406-65-1/Chlorophyll; 5712ZB110R/chlorophyll b; 9005-25-8/Starch; EC 1.13.-/Oxygenases; EC 1.13.12.-/chlorophyll a oxygenase |
| Comments/Corrections | |
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