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Title

Effect on cell wall polymers and degradability in maize mutants lacking lignin 3¿- and 5¿-O-methyl-transferases

AuthorsFornalé, Silvia ; Rencoret, Jorge ; García-Calvo, Laura; Encina, Antonio; Rigau, Joan ; Gutiérrez Suárez, Ana ; Río Andrade, José Carlos del ; Caparrós Ruiz, David
Issue Date19-Jun-2016
PublisherCSIC - Centro de Investigaciones Biológicas (CIB)
Citation4th Symposium on Biotechnology Applied to Lignocellulosics. Conference Book pág. 50 (2016)
AbstractLignin is a heterogeneous polymer produced by the oxidative polymerization of three main monolignols, p-coumaryl, coniferyl and sinapyl alcohols. When these monolignols are transported to the cell wall and polymerised, they form the so-called p-hydroxyphenyl (H), guaiacyl (G) and syringyl (S) lignin units [1-3]. Caffeoyl CoenzymeA 3-O-Methyl-Transferase (CCoAOMT) and Caffeic acid-O-Methyl-Transferase (COMT) are key enzymes in the biosynthesis of coniferyl and sinapyl alcohols. This work reports the functional characterization of these enzymes in single and double mutant maize plants. Whereas ccoaomt1 mutants show no phenotypic changes, comt and ccoaomt1 comt mutants present similar alteration patterns. Lignin content and composition remain unchanged in ccoaomt1 stems, while ccoaomt1 comt and comt stems display reduced lignin content and lower S/G ratios. The stems from all three mutants display higher hemicelluloses, ferulates and cell wall degradability. Increased cell wall degradability was observed only in ccoaomt1 comt midribs that display reduced lignin content and lower S/G ratios. Cell walls of comt midribs display lower S/G ratios and unchanged lignin content and degradability, unlike ccoaomt1 mutants whose S/G ratios remain unaffected. Our data indicate that a lower S/G ratio negatively affects the release of polysaccharides from cell walls. Interestingly, a reduction in the content of tricin, a dimethylated flavone present in the lignin polymer, was observed in the two mutants lacking COMT. This in vivo result indicates that COMT is a key enzyme required for the methylation of tricin. [1] Boerjan et al. (2003) Lignin biosynthesis. Ann. Rev. Plant Biol. 54: 519-546. [2] Ralph et al., (2004) Lignins: natural polymers from oxidative coupling of 4-hydroxyphenyl-propanoids. Phytochem. Rev. 3: 29-60. [3] Wang et al., (2013) Plant cell wall lignification and monolignol metabolism. Front. Plant Sci. 4: 220.
DescriptionComunicación presentada en el 4th Symposium on Biotechnology applied to Lignocelluloses, June 19-22, Madrid (2016)
Publisher version (URL)http://lignobiotech.es/wp-content/uploads/2016/10/Lignobiotech_IV_Madrid_2016_Conference_Book.pdf
URIhttp://hdl.handle.net/10261/158975
Appears in Collections:(CRAG) Comunicaciones congresos
(IRNAS) Comunicaciones congresos
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