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231224s2011 xx |||||o 00| ||eng c |
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|a 10.1093/jxb/err077
|2 doi
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|a pubmed24n0692.xml
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|e rakwb
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|a eng
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|a Tamasloukht, Barek
|e verfasserin
|4 aut
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|a Characterization of a cinnamoyl-CoA reductase 1 (CCR1) mutant in maize
|b effects on lignification, fibre development, and global gene expression
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|c 2011
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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 07.11.2011
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|a Date Revised 10.03.2022
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Cinnamoyl-CoA reductase (CCR), which catalyses the first committed step of the lignin-specific branch of monolignol biosynthesis, has been extensively characterized in dicot species, but few data are available in monocots. By screening a Mu insertional mutant collection in maize, a mutant in the CCR1 gene was isolated named Zmccr1(-). In this mutant, CCR1 gene expression is reduced to 31% of the residual wild-type level. Zmccr1(-) exhibited enhanced digestibility without compromising plant growth and development. Lignin analysis revealed a slight decrease in lignin content and significant changes in lignin structure. p-Hydroxyphenyl units were strongly decreased and the syringyl/guaiacyl ratio was slightly increased. At the cellular level, alterations in lignin deposition were mainly observed in the walls of the sclerenchymatic fibre cells surrounding the vascular bundles. These cell walls showed little to no staining with phloroglucinol. These histochemical changes were accompanied by an increase in sclerenchyma surface area and an alteration in cell shape. In keeping with this cell type-specific phenotype, transcriptomics performed at an early stage of plant development revealed the down-regulation of genes specifically associated with fibre wall formation. To the present authors' knowledge, this is the first functional characterization of CCR1 in a grass species
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Plant Proteins
|2 NLM
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|a Lignin
|2 NLM
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|a 9005-53-2
|2 NLM
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|a Aldehyde Oxidoreductases
|2 NLM
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|a EC 1.2.-
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|a cinnamoyl CoA reductase
|2 NLM
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|a EC 1.2.1.44
|2 NLM
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|a Wong Quai Lam, Mary Sarah-Jane
|e verfasserin
|4 aut
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|a Martinez, Yves
|e verfasserin
|4 aut
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|a Tozo, Koffi
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|4 aut
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|a Barbier, Odile
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|a Jourda, Cyril
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|a Jauneau, Alain
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|a Borderies, Gisèle
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|a Balzergue, Sandrine
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|a Renou, Jean-Pierre
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|a Huguet, Stéphanie
|e verfasserin
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|a Martinant, Jean Pierre
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|4 aut
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|a Tatout, Christophe
|e verfasserin
|4 aut
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|a Lapierre, Catherine
|e verfasserin
|4 aut
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|a Barrière, Yves
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|4 aut
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|a Goffner, Deborah
|e verfasserin
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|a Pichon, Magalie
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 62(2011), 11 vom: 14. Juli, Seite 3837-48
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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| 773 |
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|g volume:62
|g year:2011
|g number:11
|g day:14
|g month:07
|g pages:3837-48
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|u http://dx.doi.org/10.1093/jxb/err077
|3 Volltext
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