Syringyl lignin is unaltered by severe sinapyl alcohol dehydrogenase suppression in tobacco

Abdellah Barakate, Jennifer Stephens, Alison Goldie, William N Hunter, David Marshall, Robert D Hancock, Catherine Lapierre, Kris Morreel, Wout Boerjan, Claire Halpin

Research output: Contribution to journalArticleResearchpeer-review

21 Citations (Scopus)

Abstract

The manipulation of lignin could, in principle, facilitate efficient biofuel production from plant biomass. Despite intensive study of the lignin pathway, uncertainty exists about the enzyme catalyzing the last step in syringyl (S) monolignol biosynthesis, the reduction of sinapaldehyde to sinapyl alcohol. Traditional schemes of the pathway suggested that both guaiacyl (G) and S monolignols are produced by a single substrate-versatile enzyme, cinnamyl alcohol dehydrogenase (CAD). This was challenged by the discovery of a novel sinapyl alcohol dehydrogenase (SAD) that preferentially uses sinapaldehyde as a substrate and that was claimed to regulate S lignin biosynthesis in angiosperms. Consequently, most pathway schemes now show SAD (or SAD and CAD) at the sinapaldehyde reduction step, although functional evidence is lacking. We cloned SAD from tobacco (Nicotiana tabacum) and suppressed it in transgenic plants using RNA interference-inducing vectors. Characterization of lignin in the woody stems shows no change to content, composition, or structure, and S lignin is normal. By contrast, plants additionally suppressed in CAD have changes to lignin structure and S:G ratio and have increased sinapaldehyde in lignin, similar to plants suppressed in CAD alone. These data demonstrate that CAD, not SAD, is the enzyme responsible for S lignin biosynthesis in woody angiosperm xylem.

Original languageEnglish
Pages (from-to)4492-506
Number of pages15
JournalPlant Cell
Volume23
Issue number12
DOIs
Publication statusPrint publication - Dec 2011
Externally publishedYes

Fingerprint

sinapyl alcohol
Lignin
alcohol dehydrogenase
Tobacco
cinnamyl alcohol dehydrogenase
lignin
tobacco
Angiosperms
biosynthesis
Angiospermae
Enzymes
Plant RNA
Xylem
Biofuels
sinapyl alcohol dehydrogenase
enzyme substrates
Genetically Modified Plants
enzymes
RNA Interference
RNA interference

Keywords

  • Acrolein/analogs & derivatives
  • Alcohol Oxidoreductases/genetics
  • Amino Acid Sequence
  • Cloning, Molecular
  • Enzyme Activation
  • Gene Expression Regulation, Enzymologic
  • Gene Expression Regulation, Plant
  • Genes, Plant
  • Lignin/genetics
  • Microscopy, Fluorescence
  • Molecular Sequence Data
  • Phenols/metabolism
  • Phylogeny
  • Plant Proteins/genetics
  • Plant Stems/genetics
  • Plants, Genetically Modified/enzymology
  • RNA Interference
  • Recombinant Proteins/genetics
  • Substrate Specificity
  • Tobacco/enzymology
  • Wood/genetics

Cite this

Barakate, A., Stephens, J., Goldie, A., Hunter, W. N., Marshall, D., Hancock, R. D., ... Halpin, C. (2011). Syringyl lignin is unaltered by severe sinapyl alcohol dehydrogenase suppression in tobacco. Plant Cell, 23(12), 4492-506. https://doi.org/10.1105/tpc.111.089037
Barakate, Abdellah ; Stephens, Jennifer ; Goldie, Alison ; Hunter, William N ; Marshall, David ; Hancock, Robert D ; Lapierre, Catherine ; Morreel, Kris ; Boerjan, Wout ; Halpin, Claire. / Syringyl lignin is unaltered by severe sinapyl alcohol dehydrogenase suppression in tobacco. In: Plant Cell. 2011 ; Vol. 23, No. 12. pp. 4492-506.
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abstract = "The manipulation of lignin could, in principle, facilitate efficient biofuel production from plant biomass. Despite intensive study of the lignin pathway, uncertainty exists about the enzyme catalyzing the last step in syringyl (S) monolignol biosynthesis, the reduction of sinapaldehyde to sinapyl alcohol. Traditional schemes of the pathway suggested that both guaiacyl (G) and S monolignols are produced by a single substrate-versatile enzyme, cinnamyl alcohol dehydrogenase (CAD). This was challenged by the discovery of a novel sinapyl alcohol dehydrogenase (SAD) that preferentially uses sinapaldehyde as a substrate and that was claimed to regulate S lignin biosynthesis in angiosperms. Consequently, most pathway schemes now show SAD (or SAD and CAD) at the sinapaldehyde reduction step, although functional evidence is lacking. We cloned SAD from tobacco (Nicotiana tabacum) and suppressed it in transgenic plants using RNA interference-inducing vectors. Characterization of lignin in the woody stems shows no change to content, composition, or structure, and S lignin is normal. By contrast, plants additionally suppressed in CAD have changes to lignin structure and S:G ratio and have increased sinapaldehyde in lignin, similar to plants suppressed in CAD alone. These data demonstrate that CAD, not SAD, is the enzyme responsible for S lignin biosynthesis in woody angiosperm xylem.",
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Barakate, A, Stephens, J, Goldie, A, Hunter, WN, Marshall, D, Hancock, RD, Lapierre, C, Morreel, K, Boerjan, W & Halpin, C 2011, 'Syringyl lignin is unaltered by severe sinapyl alcohol dehydrogenase suppression in tobacco', Plant Cell, vol. 23, no. 12, pp. 4492-506. https://doi.org/10.1105/tpc.111.089037

Syringyl lignin is unaltered by severe sinapyl alcohol dehydrogenase suppression in tobacco. / Barakate, Abdellah; Stephens, Jennifer; Goldie, Alison; Hunter, William N; Marshall, David; Hancock, Robert D; Lapierre, Catherine; Morreel, Kris; Boerjan, Wout; Halpin, Claire.

In: Plant Cell, Vol. 23, No. 12, 12.2011, p. 4492-506.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - Syringyl lignin is unaltered by severe sinapyl alcohol dehydrogenase suppression in tobacco

AU - Barakate, Abdellah

AU - Stephens, Jennifer

AU - Goldie, Alison

AU - Hunter, William N

AU - Marshall, David

AU - Hancock, Robert D

AU - Lapierre, Catherine

AU - Morreel, Kris

AU - Boerjan, Wout

AU - Halpin, Claire

PY - 2011/12

Y1 - 2011/12

N2 - The manipulation of lignin could, in principle, facilitate efficient biofuel production from plant biomass. Despite intensive study of the lignin pathway, uncertainty exists about the enzyme catalyzing the last step in syringyl (S) monolignol biosynthesis, the reduction of sinapaldehyde to sinapyl alcohol. Traditional schemes of the pathway suggested that both guaiacyl (G) and S monolignols are produced by a single substrate-versatile enzyme, cinnamyl alcohol dehydrogenase (CAD). This was challenged by the discovery of a novel sinapyl alcohol dehydrogenase (SAD) that preferentially uses sinapaldehyde as a substrate and that was claimed to regulate S lignin biosynthesis in angiosperms. Consequently, most pathway schemes now show SAD (or SAD and CAD) at the sinapaldehyde reduction step, although functional evidence is lacking. We cloned SAD from tobacco (Nicotiana tabacum) and suppressed it in transgenic plants using RNA interference-inducing vectors. Characterization of lignin in the woody stems shows no change to content, composition, or structure, and S lignin is normal. By contrast, plants additionally suppressed in CAD have changes to lignin structure and S:G ratio and have increased sinapaldehyde in lignin, similar to plants suppressed in CAD alone. These data demonstrate that CAD, not SAD, is the enzyme responsible for S lignin biosynthesis in woody angiosperm xylem.

AB - The manipulation of lignin could, in principle, facilitate efficient biofuel production from plant biomass. Despite intensive study of the lignin pathway, uncertainty exists about the enzyme catalyzing the last step in syringyl (S) monolignol biosynthesis, the reduction of sinapaldehyde to sinapyl alcohol. Traditional schemes of the pathway suggested that both guaiacyl (G) and S monolignols are produced by a single substrate-versatile enzyme, cinnamyl alcohol dehydrogenase (CAD). This was challenged by the discovery of a novel sinapyl alcohol dehydrogenase (SAD) that preferentially uses sinapaldehyde as a substrate and that was claimed to regulate S lignin biosynthesis in angiosperms. Consequently, most pathway schemes now show SAD (or SAD and CAD) at the sinapaldehyde reduction step, although functional evidence is lacking. We cloned SAD from tobacco (Nicotiana tabacum) and suppressed it in transgenic plants using RNA interference-inducing vectors. Characterization of lignin in the woody stems shows no change to content, composition, or structure, and S lignin is normal. By contrast, plants additionally suppressed in CAD have changes to lignin structure and S:G ratio and have increased sinapaldehyde in lignin, similar to plants suppressed in CAD alone. These data demonstrate that CAD, not SAD, is the enzyme responsible for S lignin biosynthesis in woody angiosperm xylem.

KW - Acrolein/analogs & derivatives

KW - Alcohol Oxidoreductases/genetics

KW - Amino Acid Sequence

KW - Cloning, Molecular

KW - Enzyme Activation

KW - Gene Expression Regulation, Enzymologic

KW - Gene Expression Regulation, Plant

KW - Genes, Plant

KW - Lignin/genetics

KW - Microscopy, Fluorescence

KW - Molecular Sequence Data

KW - Phenols/metabolism

KW - Phylogeny

KW - Plant Proteins/genetics

KW - Plant Stems/genetics

KW - Plants, Genetically Modified/enzymology

KW - RNA Interference

KW - Recombinant Proteins/genetics

KW - Substrate Specificity

KW - Tobacco/enzymology

KW - Wood/genetics

U2 - 10.1105/tpc.111.089037

DO - 10.1105/tpc.111.089037

M3 - Article

VL - 23

SP - 4492

EP - 4506

JO - Plant Cell

JF - Plant Cell

SN - 1040-4651

IS - 12

ER -