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Bauer, S. ; Mekonnen, D.W. ; Hartmann, M.* ; Yildiz, I.* ; Janowski, R. ; Lange, B. ; Geist, B. ; Zeier, J.* ; Schäffner, A.

UGT76B1, a promiscuous hub of small molecule-based immune signaling, glucosylates N-hydroxypipecolic acid, and balances plant immunity.

Plant Cell 33, 714-734 (2021)
Verlagsversion DOI PMC
Open Access Gold (Paid Option)
Creative Commons Lizenzvertrag
Glucosylation modulates the biological activity of small molecules and frequently leads to their inactivation. The Arabidopsis thaliana glucosyltransferase UGT76B1 is involved in conjugating the stress hormone salicylic acid (SA) as well as isoleucic acid (ILA). Here, we show that UGT76B1 also glucosylates N-hydroxypipecolic acid (NHP), which is synthesized by FLAVIN-DEPENDENT MONOOXYGENASE 1 (FMO1) and activates systemic acquired resistance (SAR). Upon pathogen attack, Arabidopsis leaves generate two distinct NHP hexose conjugates, NHP-O-β-glucoside and NHP glucose ester, whereupon only NHP-O-β-glucoside formation requires a functional SA pathway. The ugt76b1 mutants specifically fail to generate the NHP-O-β-glucoside, and recombinant UGT76B1 synthesizes NHP-O-β-glucoside in vitro in competition with SA and ILA. The loss of UGT76B1 elevates the endogenous levels of NHP, SA, and ILA and establishes a constitutive SAR-like immune status. Introgression of the fmo1 mutant lacking NHP biosynthesis into the ugt76b1 background abolishes this SAR-like resistance. Moreover, overexpression of UGT76B1 in Arabidopsis shifts the NHP and SA pools toward O-β-glucoside formation and abrogates pathogen-induced SAR. Our results further indicate that NHP-triggered immunity is SA-dependent and relies on UGT76B1 as a common metabolic hub. Thereby, UGT76B1-mediated glucosylation controls the levels of active NHP, SA, and ILA in concert to balance the plant immune status.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
Schlagwörter Enhanced Disease Susceptibility; Salicylic-acid; Pipecolic Acid; Arabidopsis Mutants; Monooxygenase Fmo1; Isoleucic Acid; Resistance; Glucosyltransferase; Biosynthesis; Defense
ISSN (print) / ISBN 1040-4651
e-ISSN 1532-298X
Zeitschrift The Plant cell
Quellenangaben Band: 33, Heft: 3, Seiten: 714-734 Artikelnummer: , Supplement: ,
Verlag American Society of Plant Biologists (ASPB)
Verlagsort Journals Dept, 2001 Evans Rd, Cary, Nc 27513 Usa
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Biochemical Plant Pathology (BIOP)
Institute of Structural Biology (STB)
Förderungen Germany's Excellence Strategy
Deutsche Forschungsgemeinschaft (DFG, German Research foundation)
Helmholtz Zentrum Munchen