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Introduction of chemically labile substructures into Arabidopsis lignin through the use of LigD, the C-dehydrogenase from Sphingobium sp. strain SYK-6

Yukiko Tsuji, Ruben Vanholme UGent, Yuki Tobimatsu, Yasuyuki Ishikawa, Clifton E Foster, Naofumi Kamimura, Shojiro Hishiyama, Saki Hashimoto, Amiu Shino, Hirofumi Hara, et al. (2015) PLANT BIOTECHNOLOGY JOURNAL. 13(6). p.821-832
abstract
Bacteria-derived enzymes that can modify specific lignin substructures are potential targets to engineer plants for better biomass processability. The Gram-negative bacterium Sphingobium sp. SYK-6 possesses a C-dehydrogenase (LigD) enzyme that has been shown to oxidize the -hydroxy functionalities in -O-4-linked dimers into -keto analogues that are more chemically labile. Here, we show that recombinant LigD can oxidize an even wider range of -O-4-linked dimers and oligomers, including the genuine dilignols, guaiacylglycerol--coniferyl alcohol ether and syringylglycerol--sinapyl alcohol ether. We explored the possibility of using LigD for biosynthetically engineering lignin by expressing the codon-optimized ligD gene in Arabidopsis thaliana. The ligD cDNA, with or without a signal peptide for apoplast targeting, has been successfully expressed, and LigD activity could be detected in the extracts of the transgenic plants. UPLC-MS/MS-based metabolite profiling indicated that levels of oxidized guaiacyl (G) -O-4-coupled dilignols and analogues were significantly elevated in the LigD transgenic plants regardless of the signal peptide attachment to LigD. In parallel, 2D NMR analysis revealed a 2.1-to 2.8-fold increased level of G-type -keto--O-4 linkages in cellulolytic enzyme lignins isolated from the stem cell walls of the LigD transgenic plants, indicating that the transformation was capable of altering lignin structure in the desired manner.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
CELL-WALL, TRACHEARY ELEMENTS, FERULATE 5-HYDROXYLASE, DOWN-REGULATION, CINNAMYL ALCOHOL-DEHYDROGENASE, BETA-ARYL ETHER, SYK-6, Sphingobium sp, NMR, lignin biosynthesis, C-dehydrogenase, Arabidopsis thaliana, CARBONYL GROUPS, COA REDUCTASE, PINUS-RADIATA, POPLAR XYLEM
journal title
PLANT BIOTECHNOLOGY JOURNAL
Plant Biotechnol. J.
volume
13
issue
6
pages
821 - 832
Web of Science type
Article
Web of Science id
000357606800009
JCR category
PLANT SCIENCES
JCR impact factor
6.09 (2015)
JCR rank
11/209 (2015)
JCR quartile
1 (2015)
ISSN
1467-7644
DOI
10.1111/pbi.12316
project
Biotechnology for a sustainable economy (Bio-Economy)
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
6951512
handle
http://hdl.handle.net/1854/LU-6951512
date created
2015-10-01 14:40:35
date last changed
2016-12-19 15:41:01
@article{6951512,
  abstract     = {Bacteria-derived enzymes that can modify specific lignin substructures are potential targets to engineer plants for better biomass processability. The Gram-negative bacterium Sphingobium sp. SYK-6 possesses a C-dehydrogenase (LigD) enzyme that has been shown to oxidize the -hydroxy functionalities in -O-4-linked dimers into -keto analogues that are more chemically labile. Here, we show that recombinant LigD can oxidize an even wider range of -O-4-linked dimers and oligomers, including the genuine dilignols, guaiacylglycerol--coniferyl alcohol ether and syringylglycerol--sinapyl alcohol ether. We explored the possibility of using LigD for biosynthetically engineering lignin by expressing the codon-optimized ligD gene in Arabidopsis thaliana. The ligD cDNA, with or without a signal peptide for apoplast targeting, has been successfully expressed, and LigD activity could be detected in the extracts of the transgenic plants. UPLC-MS/MS-based metabolite profiling indicated that levels of oxidized guaiacyl (G) -O-4-coupled dilignols and analogues were significantly elevated in the LigD transgenic plants regardless of the signal peptide attachment to LigD. In parallel, 2D NMR analysis revealed a 2.1-to 2.8-fold increased level of G-type -keto--O-4 linkages in cellulolytic enzyme lignins isolated from the stem cell walls of the LigD transgenic plants, indicating that the transformation was capable of altering lignin structure in the desired manner.},
  author       = {Tsuji, Yukiko and Vanholme, Ruben and Tobimatsu, Yuki and Ishikawa, Yasuyuki and Foster, Clifton E and Kamimura, Naofumi and Hishiyama, Shojiro and Hashimoto, Saki and Shino, Amiu and Hara, Hirofumi and Sato-Izawa, Kanna and Oyarce, Paula and Goeminne, Geert and Morreel, Kris and Kikuchi, Jun and Takano, Toshiyuki and Fukuda, Masao and Katayama, Yoshihiro and Boerjan, Wout and Ralph, John and Masai, Eiji and Kajita, Shinya},
  issn         = {1467-7644},
  journal      = {PLANT BIOTECHNOLOGY JOURNAL},
  keyword      = {CELL-WALL,TRACHEARY ELEMENTS,FERULATE 5-HYDROXYLASE,DOWN-REGULATION,CINNAMYL ALCOHOL-DEHYDROGENASE,BETA-ARYL ETHER,SYK-6,Sphingobium sp,NMR,lignin biosynthesis,C-dehydrogenase,Arabidopsis thaliana,CARBONYL GROUPS,COA REDUCTASE,PINUS-RADIATA,POPLAR XYLEM},
  language     = {eng},
  number       = {6},
  pages        = {821--832},
  title        = {Introduction of chemically labile substructures into Arabidopsis lignin through the use of LigD, the C-dehydrogenase from Sphingobium sp. strain SYK-6},
  url          = {http://dx.doi.org/10.1111/pbi.12316},
  volume       = {13},
  year         = {2015},
}

Chicago
Tsuji, Yukiko, Ruben Vanholme, Yuki Tobimatsu, Yasuyuki Ishikawa, Clifton E Foster, Naofumi Kamimura, Shojiro Hishiyama, et al. 2015. “Introduction of Chemically Labile Substructures into Arabidopsis Lignin Through the Use of LigD, the C-dehydrogenase from Sphingobium Sp. Strain SYK-6.” Plant Biotechnology Journal 13 (6): 821–832.
APA
Tsuji, Y., Vanholme, R., Tobimatsu, Y., Ishikawa, Y., Foster, C. E., Kamimura, N., Hishiyama, S., et al. (2015). Introduction of chemically labile substructures into Arabidopsis lignin through the use of LigD, the C-dehydrogenase from Sphingobium sp. strain SYK-6. PLANT BIOTECHNOLOGY JOURNAL, 13(6), 821–832.
Vancouver
1.
Tsuji Y, Vanholme R, Tobimatsu Y, Ishikawa Y, Foster CE, Kamimura N, et al. Introduction of chemically labile substructures into Arabidopsis lignin through the use of LigD, the C-dehydrogenase from Sphingobium sp. strain SYK-6. PLANT BIOTECHNOLOGY JOURNAL. 2015;13(6):821–32.
MLA
Tsuji, Yukiko, Ruben Vanholme, Yuki Tobimatsu, et al. “Introduction of Chemically Labile Substructures into Arabidopsis Lignin Through the Use of LigD, the C-dehydrogenase from Sphingobium Sp. Strain SYK-6.” PLANT BIOTECHNOLOGY JOURNAL 13.6 (2015): 821–832. Print.