Ectopic Lignification in the Flax lignified bast fiber1 Mutant Stem Is Associated with Tissue-Specific Modifications in Gene Expression and Cell Wall Composition

韧皮纤维 单甘醇 亚麻 木质素 生物 次生细胞壁 人口 突变体 细胞壁 生物化学 异位表达 肉桂醇脱氢酶 木质部 植物 基因 生物合成 人口学 社会学
作者
Maxime Chantreau,Antoine Portelette,Rébecca Dauwe,Shingo Kiyoto,David Crônier,Kris Morreel,Sandrine Arribat,Godfrey Neutelings,Malika Chabi,Wout Boerjan,Arata Yoshinaga,François Mesnard,Sébastien Grec,Brigitte Chabbert,Simon Hawkins
出处
期刊:The Plant Cell [Oxford University Press]
卷期号:26 (11): 4462-4482 被引量:45
标识
DOI:10.1105/tpc.114.130443
摘要

Abstract Histochemical screening of a flax ethyl methanesulfonate population led to the identification of 93 independent M2 mutant families showing ectopic lignification in the secondary cell wall of stem bast fibers. We named this core collection the Linum usitatissimum (flax) lbf mutants for lignified bast fibers and believe that this population represents a novel biological resource for investigating how bast fiber plants regulate lignin biosynthesis. As a proof of concept, we characterized the lbf1 mutant and showed that the lignin content increased by 350% in outer stem tissues containing bast fibers but was unchanged in inner stem tissues containing xylem. Chemical and NMR analyses indicated that bast fiber ectopic lignin was highly condensed and rich in G-units. Liquid chromatography-mass spectrometry profiling showed large modifications in the oligolignol pool of lbf1 inner- and outer-stem tissues that could be related to ectopic lignification. Immunological and chemical analyses revealed that lbf1 mutants also showed changes to other cell wall polymers. Whole-genome transcriptomics suggested that ectopic lignification of flax bast fibers could be caused by increased transcript accumulation of (1) the cinnamoyl-CoA reductase, cinnamyl alcohol dehydrogenase, and caffeic acid O-methyltransferase monolignol biosynthesis genes, (2) several lignin-associated peroxidase genes, and (3) genes coding for respiratory burst oxidase homolog NADPH-oxidases necessary to increase H2O2 supply.
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