The glycosyltransferase UGT76B1 modulates N-hydroxy-pipecolic acid homeostasis and plant immunity. Issue 3 (11th January 2021)
- Record Type:
- Journal Article
- Title:
- The glycosyltransferase UGT76B1 modulates N-hydroxy-pipecolic acid homeostasis and plant immunity. Issue 3 (11th January 2021)
- Main Title:
- The glycosyltransferase UGT76B1 modulates N-hydroxy-pipecolic acid homeostasis and plant immunity
- Authors:
- Mohnike, Lennart
Rekhter, Dmitrij
Huang, Weijie
Feussner, Kirstin
Tian, Hainan
Herrfurth, Cornelia
Zhang, Yuelin
Feussner, Ivo - Abstract:
- Abstract : The UDP-dependent glycosyltransferase 76B1 influences the homeostasis of N -hydroxy-pipecolic acid in Arabidopsis thaliana by catalyzing the formation of its glycoside form. Abstract: The tradeoff between growth and defense is a critical aspect of plant immunity. Therefore, the plant immune response needs to be tightly regulated. Salicylic acid (SA) is an important plant hormone regulating defense against biotrophic pathogens. Recently, N -hydroxy-pipecolic acid (NHP) was identified as another regulator for plant innate immunity and systemic acquired resistance (SAR). Although the biosynthetic pathway leading to NHP formation is already been identified, how NHP is further metabolized is unclear. Here, we present UGT76B1 as a uridine diphosphate-dependent glycosyltransferase (UGT) that modifies NHP by catalyzing the formation of 1- O -glucosyl-pipecolic acid in Arabidopsis thaliana . Analysis of T-DNA and clustered regularly interspaced short palindromic repeats (CRISPR) knock-out mutant lines of UGT76B1 by targeted and nontargeted ultra-high performance liquid chromatography coupled to high-resolution mass spectrometry (UHPLC-HRMS) underlined NHP and SA as endogenous substrates of this enzyme in response to Pseudomonas infection and UV treatment. ugt76b1 mutant plants have a dwarf phenotype and constitutive defense response which can be suppressed by loss of function of the NHP biosynthetic enzyme FLAVIN-DEPENDENT MONOOXYGENASE 1 (FMO1). This suggests thatAbstract : The UDP-dependent glycosyltransferase 76B1 influences the homeostasis of N -hydroxy-pipecolic acid in Arabidopsis thaliana by catalyzing the formation of its glycoside form. Abstract: The tradeoff between growth and defense is a critical aspect of plant immunity. Therefore, the plant immune response needs to be tightly regulated. Salicylic acid (SA) is an important plant hormone regulating defense against biotrophic pathogens. Recently, N -hydroxy-pipecolic acid (NHP) was identified as another regulator for plant innate immunity and systemic acquired resistance (SAR). Although the biosynthetic pathway leading to NHP formation is already been identified, how NHP is further metabolized is unclear. Here, we present UGT76B1 as a uridine diphosphate-dependent glycosyltransferase (UGT) that modifies NHP by catalyzing the formation of 1- O -glucosyl-pipecolic acid in Arabidopsis thaliana . Analysis of T-DNA and clustered regularly interspaced short palindromic repeats (CRISPR) knock-out mutant lines of UGT76B1 by targeted and nontargeted ultra-high performance liquid chromatography coupled to high-resolution mass spectrometry (UHPLC-HRMS) underlined NHP and SA as endogenous substrates of this enzyme in response to Pseudomonas infection and UV treatment. ugt76b1 mutant plants have a dwarf phenotype and constitutive defense response which can be suppressed by loss of function of the NHP biosynthetic enzyme FLAVIN-DEPENDENT MONOOXYGENASE 1 (FMO1). This suggests that elevated accumulation of NHP contributes to the enhanced disease resistance in ugt76b1 . Externally applied NHP can move to distal tissue in ugt76b1 mutant plants. Although glycosylation is not required for the long-distance movement of NHP during SAR, it is crucial to balance growth and defense. … (more)
- Is Part Of:
- The Plant Cell. Volume 33:Issue 3(2021)
- Journal:
- The Plant Cell
- Issue:
- Volume 33:Issue 3(2021)
- Issue Display:
- Volume 33, Issue 3 (2021)
- Year:
- 2021
- Volume:
- 33
- Issue:
- 3
- Issue Sort Value:
- 2021-0033-0003-0000
- Page Start:
- 735
- Page End:
- 749
- Publication Date:
- 2021-01-11
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1093/plcell/koaa045 ↗
- Languages:
- English
- ISSNs:
- 1040-4651
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
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