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Title: Enzymatic basis for C‐lignin monomer biosynthesis in the seed coat of Cleome hassleriana

Journal Article · · The Plant Journal
DOI:https://doi.org/10.1111/tpj.14340· OSTI ID:1560226
 [1];  [1];  [2];  [1];  [3];  [1];  [1];  [3]; ORCiD logo [3]
  1. BioDiscovery Institute University of North Texas Denton TX USA, Department of Biological Science University of North Texas Denton TX USA
  2. BioDiscovery Institute University of North Texas Denton TX USA, Department of Biological Science University of North Texas Denton TX USA, Department of Mathematics University of North Texas Denton TX USA
  3. BioDiscovery Institute University of North Texas Denton TX USA, Department of Biological Science University of North Texas Denton TX USA, Center for Bioenergy Innovation Oak Ridge National Laboratory Oak Ridge TX USA

Summary C‐lignin is a linear polymer of caffeyl alcohol, found in the seed coats of several exotic plant species, with promising properties for generation of carbon fibers and high value chemicals. In the ornamental plant Cleome hassleriana , guaiacyl (G) lignin is deposited in the seed coat for the first 6–12 days after pollination, after which G‐lignin deposition ceases and C‐lignin accumulates, providing an excellent model system to study C‐lignin biosynthesis. We performed RNA sequencing of seed coats harvested at 2‐day intervals throughout development. Bioinformatic analysis identified a complete set of lignin biosynthesis genes for Cleome . Transcript analysis coupled with kinetic analysis of recombinant enzymes in Escherichia coli revealed that the switch to C‐lignin formation was accompanied by down‐regulation of transcripts encoding functional caffeoyl CoA‐ and caffeic acid 3‐ O ‐methyltransferases ( CC o AOMT and COMT ) and a form of cinnamyl alcohol dehydrogenase (Ch CAD 4) with preference for coniferaldehyde as substrate, and up‐regulation of a form of CAD (Ch CAD 5) with preference for caffealdehyde. Based on these analyses, blockage of lignin monomer methylation by down‐regulation of both O ‐methyltransferases ( OMT s) and methionine synthase (for provision of C1 units) appears to be the major factor in diversion of flux to C‐lignin in the Cleome seed coat, although the change in CAD specificity also contributes based on the reduction of C‐lignin levels in transgenic Cleome with down‐regulation of Ch CAD 5. Structure modeling and mutational analysis identified amino acid residues important for the preference of Ch CAD 5 for caffealdehyde.

Sponsoring Organization:
USDOE
OSTI ID:
1560226
Journal Information:
The Plant Journal, Journal Name: The Plant Journal Vol. 99 Journal Issue: 3; ISSN 0960-7412
Publisher:
Wiley-BlackwellCopyright Statement
Country of Publication:
United Kingdom
Language:
English
Citation Metrics:
Cited by: 24 works
Citation information provided by
Web of Science

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