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de Vries L, MacKay HA, Smith RA, et al. pHBMT1, a BAHD-family monolignol acyltransferase, mediates lignin acylation in poplar. Plant Physiol. 2021;doi: 10.1093/plphys/kiab546.
de Vries, L., MacKay, H. A., Smith, R. A., Mottiar, Y., Karlen, S. D., Unda, F., Muirragui, E., Bingman, C., Vander Meulen, K., Beebe, E. T., Fox, B. G., Ralph, J., & Mansfield, S. D. (2021). pHBMT1, a BAHD-family monolignol acyltransferase, mediates lignin acylation in poplar. Plant physiology, . https://doi.org/10.1093/plphys/kiab546
de Vries, Lisanne, et al. "pHBMT1, a BAHD-family monolignol acyltransferase, mediates lignin acylation in poplar." Plant physiology vol. (2021). doi: https://doi.org/10.1093/plphys/kiab546
de Vries L, MacKay HA, Smith RA, Mottiar Y, Karlen SD, Unda F, Muirragui E, Bingman C, Vander Meulen K, Beebe ET, Fox BG, Ralph J, Mansfield SD. pHBMT1, a BAHD-family monolignol acyltransferase, mediates lignin acylation in poplar. Plant Physiol. 2021 Nov 22; doi: 10.1093/plphys/kiab546. Epub 2021 Nov 22. PMID: 34977949.
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Plant Physiol. 2021 Nov 22; doi: 10.1093/plphys/kiab546. Epub 2021 Nov 22.

pHBMT1, a BAHD-family monolignol acyltransferase, mediates lignin acylation in poplar.

Plant physiology

Lisanne de Vries, Heather A MacKay, Rebecca A Smith, Yaseen Mottiar, Steven D Karlen, Faride Unda, Emilia Muirragui, Craig Bingman, Kirk Vander Meulen, Emily T Beebe, Brian G Fox, John Ralph, Shawn D Mansfield

Affiliations

  1. Department of Wood Science, Faculty of Forestry, University of British Columbia, Vancouver, BC V6T 1Z4, Canada.
  2. US Department of Energy (DOE) Great Lakes Bioenergy Research Center, the Wisconsin Energy Institute, University of Wisconsin-Madison, Madison, Wisconsin 53726, USA.
  3. Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.

PMID: 34977949 DOI: 10.1093/plphys/kiab546

Abstract

Poplar (Populus) lignin is naturally acylated with p-hydroxybenzoate ester moieties. However, the enzyme(s) involved in the biosynthesis of the monolignol-p-hydroxybenzoates have remained largely unknown. Here, we performed an in vitro screen of the Populus trichocarpa BAHD acyltransferase superfamily (116 genes) using a wheatgerm cell-free translation system and found five enzymes capable of producing monolignol-p-hydroxybenzoates. We then compared the transcript abundance of the five corresponding genes with p-hydroxybenzoate concentrations using naturally occurring unrelated genotypes of P. trichocarpa and revealed a positive correlation between the expression of p-hydroxybenzoyl-CoA monolig-nol transferase (pHBMT1, Potri.001G448000) and p-hydroxybenzoate levels. To test whether pHBMT1 is responsible for the biosynthesis of monolignol-p-hydroxybenzoates, we overexpressed pHBMT1 in hybrid poplar (Populus alba × P. grandidentata) (35S::pHBMT1 and C4H::pHBMT1). Using three complementary analytical methods, we showed that there was an increase in soluble monolignol-p-hydroxybenzoates and cell-wall-bound monolignol-p-hydroxybenzoates in the poplar transgenics. As these pendent groups are ester-linked, saponification releases p-hydroxybenzoate, a precursor to parabens that are used in pharmaceuticals and cosmetics. This identified gene could therefore be used to engineer lignocellulosic biomass with increased value for emerging biorefinery strategies.

© The Author(s) 2021. Published by Oxford University Press on behalf of American Society of Plant Biologists.

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