Identification of differentially expressed genes in sorghum (<i>Sorghum bicolor</i>) brown midrib mutants

Li, Yan; Liu, Shuwei; Zhao, S. J.; Kang, Yali; Wang, Duoxiang; Gu, Tongwei; Xin, Zhanguo; Xia, Guangmin; Huang, Yinghua

doi:10.1111/j.1399-3054.2012.01646.x

Cited by 15 publications

(5 citation statements)

References 37 publications

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“…Acetyl bromide assay to determine lignin content was performed according to a previously reported protocol [26]. The whole primary stems from 7-week-old plants were ground with liquid nitrogen and lyophilized for 48 h. Lyophilized powders were then filtered through a 425 µm screen.…”

Section: Acetyl Bromide Soluble Lignin Assay For Total Lignin Quantificationmentioning

confidence: 99%

Overexpression of pPLAIIIγ in Arabidopsis Reduced Xylem Lignification of Stem by Regulating Peroxidases

Jang

Seo

Lee

2022

Plants

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Patatin-related phospholipases A (pPLAs) are a group of plant-specific acyl lipid hydrolases that share less homology with phospholipases than that observed in other organisms. Out of the three known subfamilies (pPLAI, pPLAII, and pPLAIII), the pPLAIII member of genes is particularly known for modifying the cell wall structure, resulting in less lignin content. Overexpression of pPLAIIIα and ginseng-derived PgpPLAIIIβ in Arabidopsis and hybrid poplar was reported to reduce the lignin content. Lignin is a complex racemic phenolic heteropolymer that forms the key structural material supporting most of the tissues in plants and plays an important role in the adaptive strategies of vascular plants. However, lignin exerts a negative impact on the utilization of plant biomass in the paper and pulp industry, forage digestibility, textile industry, and production of biofuel. Therefore, the overexpression of pPLAIIIγ in Arabidopsis was analyzed in this study. This overexpression led to the formation of dwarf plants with altered anisotropic growth and reduced lignification of the stem. Transcript levels of lignin biosynthesis-related genes, as well as lignin-specific transcription factors, decreased. Peroxidase-mediated oxidation of monolignols occurs in the final stage of lignin polymerization. Two secondary cell wall-specific peroxidases were downregulated following lowered H2O2 levels, which suggests a functional role of peroxidase in the reduction of lignification by pPLAIIIγ when overexpressed in Arabidopsis.

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Section: Acetyl Bromide Soluble Lignin Assay For Total Lignin Quantificationmentioning

confidence: 99%

Overexpression of pPLAIIIγ in Arabidopsis Reduced Xylem Lignification of Stem by Regulating Peroxidases

Jang

Seo

Lee

2022

Plants

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“…A comparative analysis of lignin biosynthesis related gene families have been done across plant kingdom including sorghum (Xu et al, 2009). In sorghum, several mutants ( bmr, brown midrib , and rg, red for green ) with reduced lignin content showed increase in saccharification and digestibility compared to control plants (Palmer et al, 2008; Xin et al, 2008; Saballos et al, 2009; Yan et al, 2012; Petti et al, 2013; Sattler et al, 2014). Among these bmr mutants, several loci have been identified which includes bmr2 encoding 4-coumarate: coenzyme A ligase (4CL), bmr6 encoding cinnamyl alcohol dehydrogenase (CAD), and bmr12 and bmr18 encoding caffeic acid O-methyltransferase (COMT) enzymes of monolignol pathways (Saballos et al, 2009; Sattler et al, 2009; Scully et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

Identification, Characterization, and Expression Analysis of Cell Wall Related Genes in Sorghum bicolor (L.) Moench, a Food, Fodder, and Biofuel Crop

et al. 2016

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Biomass based alternative fuels offer a solution to the world's ever-increasing energy demand. With the ability to produce high biomass in marginal lands with low inputs, sorghum has a great potential to meet second-generation biofuel needs. Despite the sorghum crop importance in biofuel and fodder industry, there is no comprehensive information available on the cell wall related genes and gene families (biosynthetic and modification). It is important to identify the cell wall related genes to understand the cell wall biosynthetic process as well as to facilitate biomass manipulation. Genome-wide analysis using gene family specific Hidden Markov Model of conserved domains identified 520 genes distributed among 20 gene families related to biosynthesis/modification of various cell wall polymers such as cellulose, hemicellulose, pectin, and lignin. Chromosomal localization analysis of these genes revealed that about 65% of cell wall related genes were confined to four chromosomes (Chr. 1–4). Further, 56 tandem duplication events involving 169 genes were identified in these gene families which could be associated with expansion of genes within families in sorghum. Additionally, we also identified 137 Simple Sequence Repeats related to 112 genes and target sites for 10 miRNAs in some important families such as cellulose synthase, cellulose synthase-like, and laccases, etc. To gain further insight into potential functional roles, expression analysis of these gene families was performed using publically available data sets in various tissues and under abiotic stress conditions. Expression analysis showed tissue specificity as well as differential expression under abiotic stress conditions. Overall, our study provides a comprehensive information on cell wall related genes families in sorghum which offers a valuable resource to develop strategies for altering biomass composition by plant breeding and genetic engineering approaches.

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“…Of the eight sorghum PAL genes, SbPAL1 is the most highly expressed (Shakoor et al, 2014). PAL expression appears to be sensitive to perturbations in the biosynthesis of monolignols, based on semiquantitative reverse transcription-PCR analysis of 13 sorghum bmr mutants (Yan et al, 2012).…”

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confidence: 99%

Biochemical and Structural Analysis of Substrate Specificity of a Phenylalanine Ammonia-Lyase

et al. 2017

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Phenylalanine ammonia-lyase (PAL) is the first enzyme of the general phenylpropanoid pathway catalyzing the nonoxidative elimination of ammonia from l-phenylalanine to give -cinnamate. In monocots, PAL also displays tyrosine ammonia lyase (TAL) activity, leading to the formation of-coumaric acid. The catalytic mechanism and substrate specificity of a major PAL from sorghum (; SbPAL1), a strategic plant for bioenergy production, were deduced from crystal structures, molecular docking, site-directed mutagenesis, and kinetic and thermodynamic analyses. This first crystal structure of a monocotyledonous PAL displayed a unique conformation in its flexible inner loop of the 4-methylidene-imidazole-5-one (MIO) domain compared with that of dicotyledonous plants. The side chain of histidine-123 in the MIO domain dictated the distance between the catalytic MIO prosthetic group created from Ala-Ser-Gly residues and the bound l-phenylalanine and l-tyrosine, conferring the deamination reaction through either the Friedel-Crafts or E reaction mechanism. Several recombinant mutant SbPAL1 enzymes were generated via structure-guided mutagenesis, one of which, H123F-SbPAL1, has 6.2 times greater PAL activity without significant TAL activity. Additional PAL isozymes of sorghum were characterized and categorized into three groups. Taken together, this approach identified critical residues and explained substrate preferences among PAL isozymes in sorghum and other monocots, which can serve as the basis for the engineering of plants with enhanced biomass conversion properties, disease resistance, or nutritional quality.

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Identification of differentially expressed genes in sorghum (Sorghum bicolor) brown midrib mutants

Cited by 15 publications

References 37 publications

Overexpression of pPLAIIIγ in Arabidopsis Reduced Xylem Lignification of Stem by Regulating Peroxidases

Overexpression of pPLAIIIγ in Arabidopsis Reduced Xylem Lignification of Stem by Regulating Peroxidases

Identification, Characterization, and Expression Analysis of Cell Wall Related Genes in Sorghum bicolor (L.) Moench, a Food, Fodder, and Biofuel Crop

Biochemical and Structural Analysis of Substrate Specificity of a Phenylalanine Ammonia-Lyase

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