Molecular cloning, functional analysis of three cinnamyl alcohol dehydrogenase (CAD) genes in the leaves of tea plant, Camellia sinensis

Crown Copyright © 2012. Published by Elsevier GmbH. All rights reserved.

Détails bibliographiques
Publié dans:Journal of plant physiology. - 1979. - 170(2013), 3 vom: 15. Feb., Seite 272-82
Auteur principal: Deng, Wei-Wei (Auteur)
Autres auteurs: Zhang, Ming, Wu, Jian-Qiang, Jiang, Zheng-Zhong, Tang, Lei, Li, Ye-Yun, Wei, Chao-Ling, Jiang, Chang-Jun, Wan, Xiao-Chun
Format: Article en ligne
Langue:English
Publié: 2013
Accès à la collection:Journal of plant physiology
Sujets:Journal Article Research Support, Non-U.S. Gov't Acetates Cyclopentanes DNA, Plant Oxylipins Plant Growth Regulators Recombinant Proteins Abscisic Acid 72S9A8J5GW plus... methyl jasmonate 900N171A0F Alcohol Oxidoreductases EC 1.1.- cinnamyl alcohol dehydrogenase EC 1.1.1.195 Salicylic Acid O414PZ4LPZ
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100 1 |a Deng, Wei-Wei  |e verfasserin  |4 aut 
245 1 0 |a Molecular cloning, functional analysis of three cinnamyl alcohol dehydrogenase (CAD) genes in the leaves of tea plant, Camellia sinensis 
264 1 |c 2013 
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500 |a Date Completed 09.07.2013 
500 |a Date Revised 30.09.2020 
500 |a published: Print-Electronic 
500 |a Citation Status MEDLINE 
520 |a Crown Copyright © 2012. Published by Elsevier GmbH. All rights reserved. 
520 |a Cinnamyl alcohol dehydrogenase (CAD; EC 1.1.1.195) is considered to be a key enzyme in lignin biosynthesis, but little was known about CADs in tea plants (Camellia sinensis). A full-length cDNA sequence (CsCAD2) was isolated by suppressive subtractive hybridization (SSH) in Ectropis oblique feeding-induced tea plants, and another two full-length cDNA sequences (CsCAD1 and CsCAD3) were obtained from a transcriptome obtained by deep sequencing. However, they showed only 20-54% identities. Phylogenetic analysis revealed that they belonged to three different families. DNA gel blotting analysis revealed that two copies of CsCAD1 and CsCAD2 genes existed in tea genome, but CsCAD3 likely had only one copy. Recombinant proteins of these CsCADs were produced in Escherichia coli. The activity of purified recombinant CsCAD2 protein was up to 0.43 μmol min(-1) mg(-1). However, the other two recombinant proteins had lower activities, probably due to incomplete refolding. qRT-PCR analysis indicated that while CsCAD3 was strongly up-regulated in tea plants after E. oblique attack and mechanical damage, CsCAD1 and CsCAD2 showed only moderate or no changes in transcript levels. Treatment of defence-related hormones methyl jasmonate (MeJA) and salicylic acid (SA) elevated the expression of CsCAD1 and CsCAD2, but decreased the transcript abundance of CsCAD3. The transcript levels of CsCAD2 did not change after applying abscisic acid (ABA), whereas CsCAD1 and CsCAD3 were induced. These results suggested that these three CsCAD genes in tea plants may play a role in defense against insects and pathogens and adaptation to abiotic stresses and these genes likely have divergant functions 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 7 |a Acetates  |2 NLM 
650 7 |a Cyclopentanes  |2 NLM 
650 7 |a DNA, Plant  |2 NLM 
650 7 |a Oxylipins  |2 NLM 
650 7 |a Plant Growth Regulators  |2 NLM 
650 7 |a Recombinant Proteins  |2 NLM 
650 7 |a Abscisic Acid  |2 NLM 
650 7 |a 72S9A8J5GW  |2 NLM 
650 7 |a methyl jasmonate  |2 NLM 
650 7 |a 900N171A0F  |2 NLM 
650 7 |a Alcohol Oxidoreductases  |2 NLM 
650 7 |a EC 1.1.-  |2 NLM 
650 7 |a cinnamyl alcohol dehydrogenase  |2 NLM 
650 7 |a EC 1.1.1.195  |2 NLM 
650 7 |a Salicylic Acid  |2 NLM 
650 7 |a O414PZ4LPZ  |2 NLM 
700 1 |a Zhang, Ming  |e verfasserin  |4 aut 
700 1 |a Wu, Jian-Qiang  |e verfasserin  |4 aut 
700 1 |a Jiang, Zheng-Zhong  |e verfasserin  |4 aut 
700 1 |a Tang, Lei  |e verfasserin  |4 aut 
700 1 |a Li, Ye-Yun  |e verfasserin  |4 aut 
700 1 |a Wei, Chao-Ling  |e verfasserin  |4 aut 
700 1 |a Jiang, Chang-Jun  |e verfasserin  |4 aut 
700 1 |a Wan, Xiao-Chun  |e verfasserin  |4 aut 
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