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Broadening the roles of UDP-glycosyltransferases in auxin homeostasis and plant development.
Mateo-Bonmatí, Eduardo; Casanova-Sáez, Rubén; Simura, Jan; Ljung, Karin.
Afiliación
  • Mateo-Bonmatí E; Umeå Plant Science Centre, Department of Forest Genetics and Plant Physiology, Swedish University of Agricultural Sciences, Umeå, SE-901 83, Sweden.
  • Casanova-Sáez R; Umeå Plant Science Centre, Department of Forest Genetics and Plant Physiology, Swedish University of Agricultural Sciences, Umeå, SE-901 83, Sweden.
  • Simura J; Umeå Plant Science Centre, Department of Forest Genetics and Plant Physiology, Swedish University of Agricultural Sciences, Umeå, SE-901 83, Sweden.
  • Ljung K; Umeå Plant Science Centre, Department of Forest Genetics and Plant Physiology, Swedish University of Agricultural Sciences, Umeå, SE-901 83, Sweden.
New Phytol ; 232(2): 642-654, 2021 10.
Article en En | MEDLINE | ID: mdl-34289137
ABSTRACT
The levels of the important plant growth regulator indole-3-acetic acid (IAA) are tightly controlled within plant tissues to spatiotemporally orchestrate concentration gradients that drive plant growth and development. Metabolic inactivation of bioactive IAA is known to participate in the modulation of IAA maxima and minima. IAA can be irreversibly inactivated by oxidation and conjugation to aspartate and glutamate. Usually overlooked because of its reversible nature, the most abundant inactive IAA form is the IAA-glucose (IAA-glc) conjugate. Glycosylation of IAA in Arabidopsis thaliana is reported to be carried out by UDP-glycosyltransferase 84B1 (UGT84B1), while UGT74D1 has been implicated in the glycosylation of the irreversibly formed IAA catabolite oxIAA. Here we demonstrated that both UGT84B1 and UGT74D1 modulate IAA levels throughout plant development by dual IAA and oxIAA glycosylation. Moreover, we identified a novel UGT subfamily whose members redundantly mediate the glycosylation of oxIAA and modulate skotomorphogenic growth.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Glicosiltransferasas / Proteínas de Arabidopsis Idioma: En Revista: New Phytol Asunto de la revista: BOTANICA Año: 2021 Tipo del documento: Article País de afiliación: Suecia

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Glicosiltransferasas / Proteínas de Arabidopsis Idioma: En Revista: New Phytol Asunto de la revista: BOTANICA Año: 2021 Tipo del documento: Article País de afiliación: Suecia