A Wheat Cinnamyl Alcohol Dehydrogenase TaCAD12 Contributes to Host Resistance to the Sharp Eyespot Disease

Rong, Wei; Luo, Meiying; Shan, Tianlei; Wei, Xuening; Du, Liangcheng; Xu, Huijun; Zhang, Zengyan

doi:10.3389/fpls.2016.01723

Cited by 49 publications

(41 citation statements)

References 51 publications

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“…In conclusion, CAD genes play significant role in various metabolic pathways such as lignification, pathogen defense, growth, and abiotic and biotic stress mechanism [39]. Consequently, the results presented here support to understand CAD genes functions in various biological processes in plants and to contribute to in silico and experimental studies about CADs involvement to these processes.…”

Section: The Gene Structure and Phylogenetic Analysis Of Plant Cadssupporting

confidence: 69%

Bioinformatical Analyses of cinnamyl alcohol dehydrogenase (CAD) proteins from higher plant species

Kurt

Filiz²

2019

Bitlis Eren Üniversitesi Fen Bilimleri Dergisi

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Cinnamyl alcohol dehydrogenase (CAD) (EC 1.1.1.195) is an enzyme functioning in the reduction of various phenylpropenyl aldehyde derivatives which are precursors in lignin and lignan production. Species-specific CAD genes have been extensively identified in recent years. In this study, we used bioinformatics tools to characterize and classify plant CADs. The amino acid and nucleotide sequences of 16 CADs from different plant species were used to compare their physiological properties, phylogeny, and conserved motifs. For this purpose, sequence, phylogenetical, structural analyses of proteins were conducted using various servers. All plant CADs had the characteristic alcohol dehydrogenase (PF08240) and zinc-binding dehydrogenase domains (PF00107). According to the physicochemical analysis, it was revealed that the most of plant CADs (81.25%) were in acidic character. Sequence length (aa) and molecular weight (kDa) of CAD proteins were found in range of 356-367 and 38.6-40.5 respectively. The highest sequence similarities were found between Sorghum bicolor and Zea mays (95.3%), Panicum virgatum and Sorghum bicolor (90.9%), and Oryza sativa and Zea mays (87.1%) respectively. Plant CADs showed divergent exon-intron structures in which exon numbers were ranged from two to six. Four monocot species (S. bicolor, P. virgatum, Z. mays, and O. sativa) have four exons, whereas Brachypodium distachyon contains only two exons. Phylogenetic analysis revealed that the CAD proteins mainly divided into two groups. The highest bootstrap values were found as follows: Fragaria vesca-Prunus persica clade (100%), Glycine max-Medicago truncatula (81%), and S. bicolor-Z. mays (72%). The 3D structures of plant CADs showed that Oryza and Vitis had the most divergent structures when compared to the other plant species. Eventually, the data represented here contribute to studies aiming at evaluating the plant CADs extensively and at identifying new CAD genes in other plants.

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Section: The Gene Structure and Phylogenetic Analysis Of Plant Cadssupporting

confidence: 69%

Bioinformatical Analyses of cinnamyl alcohol dehydrogenase (CAD) proteins from higher plant species

Kurt

Filiz²

2019

Bitlis Eren Üniversitesi Fen Bilimleri Dergisi

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“…Although PbCAD3 belongs to the bona fide CAD clade, its expression level was much weaker in fruits than in buds. Therefore, PbCAD3 may not be responsible for lignin biosynthesis in fruit, or it may be induced under specific circumstances such as insect attack or other damage ( Rong et al, 2016 ). Similar expression levels were found for PbCAD7 and - 9 in fruit, and the trends of PbCAD1 , - 19 and - 25 expression were not significantly correlated with lignin and stone cell contents.…”

Section: Resultsmentioning

confidence: 99%

Characterization and analysis of CCR and CAD gene families at the whole-genome level for lignin synthesis of stone cells in pear (Pyrus bretschneideri) fruit

Cheng

et al. 2017

Biology Open

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The content of stone cells has significant effects on the flavour and quality of pear fruit. Previous research suggested that lignin deposition is closely related to stone cell formation. In the lignin biosynthetic pathway, cinnamoyl-CoA reductase (CCR) and cinnamyl alcohol dehydrogenase (CAD), dehydrogenase/reductase family members, catalyse the last two steps in monolignol synthesis. However, there is little knowledge of the characteristics of the CCR and CAD families in pear and their involvement in lignin synthesis of stone cells. In this study, 31 CCRs and 26 CADs were identified in the pear genome. Phylogenetic trees for CCRs and CADs were constructed; key amino acid residues were analysed, and three-dimensional structures were predicted. Using quantitative real-time polymerase chain reaction (qRT-PCR), PbCAD2, PbCCR1, -2 and -3 were identified as participating in lignin synthesis of stone cells in pear fruit. Subcellular localization analysis showed that the expressed proteins (PbCAD2, PbCCR1, -2 and -3) are found in the cytoplasm or at the cell membrane. These results reveal the evolutionary features of the CCR and CAD families in pear as well as the genes responsible for regulation of lignin synthesis and stone cell development in pear fruit.

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“…Therefore, molecular breeding is important to uncover the mechanism of wheat defense against R. cerealis and to identify new resistance regulators from the wheat genome. Previous studies in Zhang’s laboratory have identified several genes that are involved in wheat defense response against R. cerealis , such as TaPIE1 ( Zhu et al, 2014 ), TaAGC1 ( Zhu et al, 2015 ), TaCAD12 ( Rong et al, 2016 ), and TaRCR1 ( Zhu et al, 2017 ). However, no study about the role of PP2A in wheat defense responses to pathogens has been reported yet.…”

Section: Introductionmentioning

confidence: 99%

Silencing of the Wheat Protein Phosphatase 2A Catalytic Subunit TaPP2Ac Enhances Host Resistance to the Necrotrophic Pathogen Rhizoctonia cerealis

Zhu

Wang

et al. 2018

Front. Plant Sci.

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Eukaryotic type 2A protein phosphatases (protein phosphatase 2A, PP2A) consist of a scaffold subunit A, a regulatory subunit B, and a catalytic subunit C. Little is known about the roles of PP2Ac proteins that are involved in plant responses to necrotrophic fungal pathogens. Sharp eyespot, caused by the necrotrophic fungus Rhizoctonia cerealis, is a destructive disease of wheat (Triticum aestivum), an important staple food crop. Here, we isolated TaPP2Ac-4D from wheat, which encodes a catalytic subunit of the heterotrimeric PP2A, and characterized its properties and role in plant defense response to R. cerealis. Based on the sequence alignment of TaPP2Ac-4D with the draft sequences of wheat chromosomes from the International Wheat Genome Sequencing Consortium (IWGSC), it was found that TaPP2Ac-4D gene is located on the long arm of the wheat chromosome 4D and has two homologs assigned on wheat chromosomes 4A and 4B. Sequence and phylogenetic tree analyses revealed that the TaPP2Ac protein is a typical member of the PP2Ac family and belongs to the subfamily II. TaPP2Ac-4B and TaPP2Ac-4D displayed higher transcriptional levels in the R. cerealis-susceptible wheat cultivar Wenmai 6 than those seen in the resistant wheat line CI12633. The transcriptional levels of TaPP2Ac-4B and TaPP2Ac-4D were significantly elevated in wheat R. cerealis after infection and upon H2O2 treatment. Virus-induced gene silencing results revealed that the transcriptional knockdown of TaPP2Ac-4D and TaPP2Ac-4B significantly increased wheat resistance to R. cerealis infection. Meanwhile, the transcriptional levels of certain pathogenesis-related (PR) and reactive oxygen species (ROS)-scavenging enzyme encoding genes were increased in TaPP2Ac-silenced wheat plants. These results suggest that TaPP2Ac-4B and TaPP2Ac-4D negatively regulate defense response to R. cerealis infection possibly through modulation of the expression of certain PR and ROS-scavenging enzyme genes in wheat. This study reveals a novel function of the plant PP2Ac genes in plant immune responses.

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A Wheat Cinnamyl Alcohol Dehydrogenase TaCAD12 Contributes to Host Resistance to the Sharp Eyespot Disease

Cited by 49 publications

References 51 publications

Bioinformatical Analyses of cinnamyl alcohol dehydrogenase (CAD) proteins from higher plant species

Bioinformatical Analyses of cinnamyl alcohol dehydrogenase (CAD) proteins from higher plant species

Characterization and analysis of CCR and CAD gene families at the whole-genome level for lignin synthesis of stone cells in pear (Pyrus bretschneideri) fruit

Silencing of the Wheat Protein Phosphatase 2A Catalytic Subunit TaPP2Ac Enhances Host Resistance to the Necrotrophic Pathogen Rhizoctonia cerealis

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