p HBMT1, a BAHD-family monolignol acyltransferase, mediates lignin acylation in poplar

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

doi:10.1093/plphys/kiab546

Title: p HBMT1, a BAHD-family monolignol acyltransferase, mediates lignin acylation in poplar

Journal Article · Mon Nov 22 00:00:00 UTC 2021 · Plant Physiology (Bethesda)

DOI: https://doi.org/10.1093/plphys/kiab546 · OSTI ID:1844039

; MacKay, Heather A.;

;

; Muirragui, Emilia; Bingman, Craig; Vander Meulen, Kirk; Beebe, Emily T.; Fox, Brian G.;

;

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.

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Research Organization:: Great Lakes Bioenergy Research Center (GLBRC), Madison, WI (United States); University of Wisconsin, Madison, WI (United States); University of Wisconsin-Madison, WI (United States)

Sponsoring Organization:: USDOE; USDOE Office of Science (SC); USDOE Office of Science (SC), Biological and Environmental Research (BER)

Grant/Contract Number:: SC0018409; SC0020349; SC0023049

OSTI ID:: 1844039

Journal Information:: Plant Physiology (Bethesda), Journal Name: Plant Physiology (Bethesda) Journal Issue: 2 Vol. 188; ISSN 0032-0889

Publisher:: Oxford University PressCopyright Statement

Country of Publication:: United States

Language:: English

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