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Title: SbCOMT (Bmr12) is involved in the biosynthesis of tricin-lignin in sorghum

Abstract

Lignin in plant biomass represents a target for engineering strategies towards the development of a sustainable bioeconomy. In addition to the conventional lignin monomers, namely p-coumaryl, coniferyl and sinapyl alcohols, tricin has been shown to be part of the native lignin polymer in certain monocot species. Because tricin is considered to initiate the polymerization of lignin chains, elucidating its biosynthesis and mechanism of export to the cell wall constitute novel challenges for the engineering of bioenergy crops. Late steps of tricin biosynthesis require two methylation reactions involving the pathway intermediate selgin. It has recently been demonstrated in rice and maize that caffeate O-methyltransferase (COMT) involved in the synthesis syringyl (S) lignin units derived from sinapyl alcohol also participates in the synthesis of tricin in planta. In this work, we validate in sorghum (Sorghum bicolor L.) that the O-methyltransferase responsible for the production of S lignin units (SbCOMT / Bmr12) is also involved in the synthesis of lignin-linked tricin. In particular, we show that biomass from the sorghum bmr12 mutant contains lower level of tricin incorporated into lignin, and that SbCOMT can methylate the tricin precursors luteolin and selgin. Our genetic and biochemical data point toward a general mechanism whereby COMTmore » is involved in the synthesis of both tricin and S lignin units.« less

Authors:
 [1];  [2];  [3];  [4];  [5];  [6];  [6];  [7];  [8];  [9];  [2];  [6]; ORCiD logo [10];  [11]
  1. Joint BioEnergy Inst. (JBEI), Emeryville, CA (United States); Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Environmental Genomics and Systems Biology Division
  2. Joint BioEnergy Inst. (JBEI), Emeryville, CA (United States); Sandia National Lab. (SNL-CA), Livermore, CA (United States). Biomass Science and Conversion Technology Dept.
  3. Joint BioEnergy Inst. (JBEI), Emeryville, CA (United States); Sandia National Lab. (SNL-CA), Livermore, CA (United States). Biotechnology and Bioengineering Dept.
  4. Joint BioEnergy Inst. (JBEI), Emeryville, CA (United States); Univ. of Liege (Belgium). Lab. of Biological and Industrial Chemistry
  5. Joint BioEnergy Inst. (JBEI), Emeryville, CA (United States); Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Environmental Genomics and Systems Biology Division; Univ. of California, Berkeley, CA (United States). Dept. of Molecular and Cell Biology
  6. Joint BioEnergy Inst. (JBEI), Emeryville, CA (United States); Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Biological Systems and Engineering Division
  7. Univ. of Liege (Belgium). Lab. of Biological and Industrial Chemistry
  8. Wheat, Sorghum and Forage Research Univ., Lincoln, NE (United States)
  9. Joint BioEnergy Inst. (JBEI), Emeryville, CA (United States); Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Environmental Genomics and Systems Biology Division; USDOE Joint Genome Institute (JGI), Walnut Creek, CA (United States)
  10. Joint BioEnergy Inst. (JBEI), Emeryville, CA (United States); Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Environmental Genomics and Systems Biology Division; Univ. of California, Berkeley, CA (United States). Dept. of Plant and Microbial Biology; Univ. of Lyon (France)
  11. Tallinn Univ. of Technology (Estonia)
Publication Date:
Research Org.:
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Sponsoring Org.:
USDOE Office of Science (SC)
OSTI Identifier:
1361947
Alternate Identifier(s):
OSTI ID: 1379876
Grant/Contract Number:  
AC02-05CH11231
Resource Type:
Journal Article: Published Article
Journal Name:
PLoS ONE
Additional Journal Information:
Journal Volume: 12; Journal Issue: 6; Journal ID: ISSN 1932-6203
Publisher:
Public Library of Science
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Eudes, Aymerick, Dutta, Tanmoy, Deng, Kai, Jacquet, Nicolas, Sinha, Anagh, Benites, Veronica T., Baidoo, Edward E. K., Richel, Aurore, Sattler, Scott E., Northen, Trent R., Singh, Seema, Simmons, Blake A., Loqué, Dominique, and Gupta, Vijai. SbCOMT (Bmr12) is involved in the biosynthesis of tricin-lignin in sorghum. United States: N. p., 2017. Web. doi:10.1371/journal.pone.0178160.
Eudes, Aymerick, Dutta, Tanmoy, Deng, Kai, Jacquet, Nicolas, Sinha, Anagh, Benites, Veronica T., Baidoo, Edward E. K., Richel, Aurore, Sattler, Scott E., Northen, Trent R., Singh, Seema, Simmons, Blake A., Loqué, Dominique, & Gupta, Vijai. SbCOMT (Bmr12) is involved in the biosynthesis of tricin-lignin in sorghum. United States. doi:10.1371/journal.pone.0178160.
Eudes, Aymerick, Dutta, Tanmoy, Deng, Kai, Jacquet, Nicolas, Sinha, Anagh, Benites, Veronica T., Baidoo, Edward E. K., Richel, Aurore, Sattler, Scott E., Northen, Trent R., Singh, Seema, Simmons, Blake A., Loqué, Dominique, and Gupta, Vijai. Thu . "SbCOMT (Bmr12) is involved in the biosynthesis of tricin-lignin in sorghum". United States. doi:10.1371/journal.pone.0178160.
@article{osti_1361947,
title = {SbCOMT (Bmr12) is involved in the biosynthesis of tricin-lignin in sorghum},
author = {Eudes, Aymerick and Dutta, Tanmoy and Deng, Kai and Jacquet, Nicolas and Sinha, Anagh and Benites, Veronica T. and Baidoo, Edward E. K. and Richel, Aurore and Sattler, Scott E. and Northen, Trent R. and Singh, Seema and Simmons, Blake A. and Loqué, Dominique and Gupta, Vijai},
abstractNote = {Lignin in plant biomass represents a target for engineering strategies towards the development of a sustainable bioeconomy. In addition to the conventional lignin monomers, namely p-coumaryl, coniferyl and sinapyl alcohols, tricin has been shown to be part of the native lignin polymer in certain monocot species. Because tricin is considered to initiate the polymerization of lignin chains, elucidating its biosynthesis and mechanism of export to the cell wall constitute novel challenges for the engineering of bioenergy crops. Late steps of tricin biosynthesis require two methylation reactions involving the pathway intermediate selgin. It has recently been demonstrated in rice and maize that caffeate O-methyltransferase (COMT) involved in the synthesis syringyl (S) lignin units derived from sinapyl alcohol also participates in the synthesis of tricin in planta. In this work, we validate in sorghum (Sorghum bicolor L.) that the O-methyltransferase responsible for the production of S lignin units (SbCOMT / Bmr12) is also involved in the synthesis of lignin-linked tricin. In particular, we show that biomass from the sorghum bmr12 mutant contains lower level of tricin incorporated into lignin, and that SbCOMT can methylate the tricin precursors luteolin and selgin. Our genetic and biochemical data point toward a general mechanism whereby COMT is involved in the synthesis of both tricin and S lignin units.},
doi = {10.1371/journal.pone.0178160},
journal = {PLoS ONE},
number = 6,
volume = 12,
place = {United States},
year = {Thu Jun 08 00:00:00 EDT 2017},
month = {Thu Jun 08 00:00:00 EDT 2017}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record at 10.1371/journal.pone.0178160

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Cited by: 3 works
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