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231224s2015 xx |||||o 00| ||eng c |
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|a 10.1093/jxb/eru457
|2 doi
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|a pubmed24n0814.xml
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|a (DE-627)NLM244228922
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|a (NLM)25468933
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
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|a Wang, Yong
|e verfasserin
|4 aut
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|a FAR5, a fatty acyl-coenzyme A reductase, is involved in primary alcohol biosynthesis of the leaf blade cuticular wax in wheat (Triticum aestivum L.)
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|c 2015
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 13.01.2016
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|a Date Revised 13.11.2018
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a © The Author 2014. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com.
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|a A waxy cuticle that serves as a protective barrier against non-stomatal water loss and environmental damage coats the aerial surfaces of land plants. It comprises a cutin polymer matrix and waxes. Cuticular waxes are complex mixtures of very long chain fatty acids (VLCFAs) and their derivatives. Results show that primary alcohols are the major components of bread wheat (Triticum aestivum L.) leaf blade cuticular waxes. Here, the characterization of TaFAR5 from wheat cv Xinong 2718, which is allelic to TAA1b, an anther-specific gene, is reported. Evidence is presented for a new function for TaFAR5 in the biosynthesis of primary alcohols of leaf blade cuticular wax in wheat. Expression of TaFAR5 cDNA in yeast (Saccharomyces cerevisiae) led to production of C22:0 primary alcohol. The transgenic expression of TaFAR5 in tomato (Solanum lycopersicum) cv MicroTom leaves resulted in the accumulation of C26:0, C28:0, and C30:0 primary alcohols. TaFAR5 encodes an alcohol-forming fatty acyl-coenzyme A reductase (FAR). Expression analysis revealed that TaFAR5 was expressed at high levels in the leaf blades, anthers, pistils, and seeds. Fully functional green fluorescent protein-tagged TaFAR5 protein was localized to the endoplasmic reticulum (ER), the site of primary alcohol biosynthesis. SDS-PAGE analysis indicated that the TaFAR5 protein possessed a molecular mass of 58.4kDa, and it was also shown that TaFAR5 transcript levels were regulated in response to drought, cold, and abscisic acid (ABA). Overall, these data suggest that TaFAR5 plays an important role in the synthesis of primary alcohols in wheat leaf blade
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Abiotic stress
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|a cuticular wax
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|a endoplasmic reticulum
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|a fatty acid
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|a fatty acyl-CoA reductase
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|a leaf blade
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|a primary alcohol
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|a wheat.
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|a Alcohols
|2 NLM
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|a Plant Proteins
|2 NLM
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|a Waxes
|2 NLM
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|a Aldehyde Oxidoreductases
|2 NLM
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|a EC 1.2.-
|2 NLM
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|a hexadecanal dehydrogenase (acylating)
|2 NLM
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|a EC 1.2.1.42
|2 NLM
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| 700 |
1 |
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|a Wang, Meiling
|e verfasserin
|4 aut
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|a Sun, Yulin
|e verfasserin
|4 aut
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|a Wang, Yanting
|e verfasserin
|4 aut
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|a Li, Tingting
|e verfasserin
|4 aut
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|a Chai, Guaiqiang
|e verfasserin
|4 aut
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|a Jiang, Wenhui
|e verfasserin
|4 aut
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|a Shan, Liwei
|e verfasserin
|4 aut
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|a Li, Chunlian
|e verfasserin
|4 aut
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|a Xiao, Enshi
|e verfasserin
|4 aut
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|a Wang, Zhonghua
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 66(2015), 5 vom: 27. März, Seite 1165-78
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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| 773 |
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|g volume:66
|g year:2015
|g number:5
|g day:27
|g month:03
|g pages:1165-78
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|u http://dx.doi.org/10.1093/jxb/eru457
|3 Volltext
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|d 66
|j 2015
|e 5
|b 27
|c 03
|h 1165-78
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