Substrate Specificity of LACCASE8 Facilitates Polymerization of Caffeyl Alcohol for C-Lignin Biosynthesis in the Seed Coat of Cleome hassleriana . Issue 12 (9th October 2020)
- Record Type:
- Journal Article
- Title:
- Substrate Specificity of LACCASE8 Facilitates Polymerization of Caffeyl Alcohol for C-Lignin Biosynthesis in the Seed Coat of Cleome hassleriana . Issue 12 (9th October 2020)
- Main Title:
- Substrate Specificity of LACCASE8 Facilitates Polymerization of Caffeyl Alcohol for C-Lignin Biosynthesis in the Seed Coat of Cleome hassleriana
- Authors:
- Wang, Xin
Zhuo, Chunliu
Xiao, Xirong
Wang, Xiaoqiang
Docampo-Palacios, Maite
Chen, Fang
Dixon, Richard A. - Abstract:
- Abstract : LACCASE8 from the model system Cleome hassleriana possesses the unusual property of oxidizing caffeyl alcohol but not coniferyl alcohol and plays a critical role in initiating C-lignin polymerization. Abstract: Catechyl lignin (C-lignin) is a linear homopolymer of caffeyl alcohol found in the seed coats of diverse plant species. Its properties make it a natural source of carbon fibers and high-value chemicals, but the mechanism of in planta polymerization of caffeyl alcohol remains unclear. In the ornamental plant Cleome hassleriana, lignin biosynthesis in the seed coat switches from guaiacyl lignin to C-lignin at ∼12 d after pollination. Here we found that the transcript profile of the laccase gene ChLAC8 parallels the accumulation of C-lignin during seed coat development. Recombinant ChLAC8 oxidizes caffeyl and sinapyl alcohols, generating their corresponding dimers or trimers in vitro, but cannot oxidize coniferyl alcohol. We propose a basis for this substrate preference based on molecular modeling/docking experiments. Suppression of ChLAC8 expression led to significantly reduced C-lignin content in the seed coats of transgenic Cleome plants. Feeding of 13 C-caffeyl alcohol to the Arabidopsis ( Arabidopsis thaliana ) caffeic acid o - methyltransferase mutant resulted in no incorporation of 13 C into C-lignin, but expressing ChLAC8 in this genetic background led to appearance of C-lignin with >40% label incorporation. These results indicate that ChLAC8 isAbstract : LACCASE8 from the model system Cleome hassleriana possesses the unusual property of oxidizing caffeyl alcohol but not coniferyl alcohol and plays a critical role in initiating C-lignin polymerization. Abstract: Catechyl lignin (C-lignin) is a linear homopolymer of caffeyl alcohol found in the seed coats of diverse plant species. Its properties make it a natural source of carbon fibers and high-value chemicals, but the mechanism of in planta polymerization of caffeyl alcohol remains unclear. In the ornamental plant Cleome hassleriana, lignin biosynthesis in the seed coat switches from guaiacyl lignin to C-lignin at ∼12 d after pollination. Here we found that the transcript profile of the laccase gene ChLAC8 parallels the accumulation of C-lignin during seed coat development. Recombinant ChLAC8 oxidizes caffeyl and sinapyl alcohols, generating their corresponding dimers or trimers in vitro, but cannot oxidize coniferyl alcohol. We propose a basis for this substrate preference based on molecular modeling/docking experiments. Suppression of ChLAC8 expression led to significantly reduced C-lignin content in the seed coats of transgenic Cleome plants. Feeding of 13 C-caffeyl alcohol to the Arabidopsis ( Arabidopsis thaliana ) caffeic acid o - methyltransferase mutant resulted in no incorporation of 13 C into C-lignin, but expressing ChLAC8 in this genetic background led to appearance of C-lignin with >40% label incorporation. These results indicate that ChLAC8 is required for C-lignin polymerization and determines lignin composition when caffeyl alcohol is available. … (more)
- Is Part Of:
- The Plant Cell. Volume 32:Issue 12(2020)
- Journal:
- The Plant Cell
- Issue:
- Volume 32:Issue 12(2020)
- Issue Display:
- Volume 32, Issue 12 (2020)
- Year:
- 2020
- Volume:
- 32
- Issue:
- 12
- Issue Sort Value:
- 2020-0032-0012-0000
- Page Start:
- 3825
- Page End:
- 3845
- Publication Date:
- 2020-10-09
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1105/tpc.20.00598 ↗
- Languages:
- English
- ISSNs:
- 1040-4651
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 16495.xml