Suppression of CINNAMOYL-CoA REDUCTASE increases the level of monolignol ferulates incorporated into maize lignins

Creators

Shawn M. Kaeppler, Department of Agronomy, University of Wisconsin-Madison
John C. Sedbrook, Department of Energy Great Lakes Bioenergy Research Center, School of Biological Sciences, Illinois State University
Cynthia L. Cass, Department of Energy Great Lakes Bioenergy Research Center, School of Biological Sciences, Illinois State University
Rebecca A. Smith, Department of Biochemistry, University of Wisconsin-Madison
Heidi Kaeppler, Department of Agronomy, University of Wisconsin-Madison
Steven D. Karlen, Department of Biochemistry, University of Wisconsin-Madison
Shawn D. Mansfield, Department of Wood Science, University of British Columbia
Rajandeep S. Sekhon, Department of Genetics and Biochemistry, Clemson University
Natalia De Leon, Department of Agronomy, University of Wisconsin-Madison
Marlies Heckwolf, Department of Energy Great Lakes Bioenergy Research Center, Wisconsin Energy Institute, University of Wisconsin-Madison
John Ralph, Department of Biochemistry, University of Wisconsin-Madison
Mona Mazaheri, Department of Energy Great Lakes Bioenergy Research Center, Wisconsin Energy Institute, University of Wisconsin-Madison

Description

Abstract Background The cell wall polymer lignin provides structural support and rigidity to plant cell walls, and therefore to the plant body. However, the recalcitrance associated with lignin impedes the extraction of polysaccharides from the cell wall to make plant-based biofuels and biomaterials. The cell wall digestibility can be improved by introducing labile ester bonds into the lignin backbone that can be easily broken under mild base treatment at room temperature. The FERULOYL-CoA MONOLIGNOL TRANSFERASE (FMT) enzyme, which may be naturally found in many plants, uses feruloyl-CoA and monolignols to synthesize the ester-linked monolignol ferulate conjugates. A mutation in the first lignin-specific biosynthetic enzyme, CINNAMOYL-CoA REDUCTASE (CCR), results in an increase in the intracellular pool of feruloyl-CoA. Results Maize (Zea mays) has a native putative FMT enzyme, and its ccr mutants produce an increased pool of feruloyl-CoA that can be used for conversion to monolignol ferulate conjugates. The decreased lignin content and monomers did not, however, impact the plant growth or biomass. The increase in monolignol conjugates correlated with an improvement in the digestibility of maize stem rind tissue. Conclusions Together, increased monolignol ferulates and improved digestibility in ccr1 mutant plants suggests that they may be superior biofuel crops.

Publication Date

1-1-2017

Publisher

figshare Academic Research System

DOI

10.6084/m9.figshare.c.3769808.v1

Document Type

Data Set

Recommended Citation

Kaeppler, Shawn M.; Sedbrook, John C.; Cass, Cynthia L.; Smith, Rebecca A.; Kaeppler, Heidi; Karlen, Steven D.; Mansfield, Shawn D.; Sekhon, Rajandeep S.; De Leon, Natalia; Heckwolf, Marlies; Ralph, John; Mazaheri, Mona (2017), "Suppression of CINNAMOYL-CoA REDUCTASE increases the level of monolignol ferulates incorporated into maize lignins", figshare Academic Research System, doi: 10.6084/m9.figshare.c.3769808.v1

https://doi.org/10.6084/m9.figshare.c.3769808.v1

Identifier

10.6084/m9.figshare.c.3769808.v1

Related Content

10.1186/s13068-017-0793-1

Embargo Date

1-1-2017