Identification of tomato F-box proteins functioning in phenylpropanoid metabolism.


Journal

Plant molecular biology
ISSN: 1573-5028
Titre abrégé: Plant Mol Biol
Pays: Netherlands
ID NLM: 9106343

Informations de publication

Date de publication:
12 Jul 2024
Historique:
received: 07 04 2024
accepted: 26 06 2024
medline: 12 7 2024
pubmed: 12 7 2024
entrez: 12 7 2024
Statut: epublish

Résumé

Phenylpropanoids, a class of specialized metabolites, play crucial roles in plant growth and stress adaptation and include diverse phenolic compounds such as flavonoids. Phenylalanine ammonia-lyase (PAL) and chalcone synthase (CHS) are essential enzymes functioning at the entry points of general phenylpropanoid biosynthesis and flavonoid biosynthesis, respectively. In Arabidopsis, PAL and CHS are turned over through ubiquitination-dependent proteasomal degradation. Specific kelch domain-containing F-Box (KFB) proteins as components of ubiquitin E3 ligase directly interact with PAL or CHS, leading to polyubiquitinated PAL and CHS, which in turn influences phenylpropanoid and flavonoid production. Although phenylpropanoids are vital for tomato nutritional value and stress responses, the post-translational regulation of PAL and CHS in tomato remains unknown. We identified 31 putative KFB-encoding genes in the tomato genome. Our homology analysis and phylogenetic study predicted four PAL-interacting SlKFBs, while SlKFB18 was identified as the sole candidate for the CHS-interacting KFB. Consistent with their homolog function, the predicted four PAL-interacting SlKFBs function in PAL degradation. Surprisingly, SlKFB18 did not interact with tomato CHS and the overexpression or knocking out of SlKFB18 did not affect phenylpropanoid contents in tomato transgenic lines, suggesting its irreverence with flavonoid metabolism. Our study successfully discovered the post-translational regulatory machinery of PALs in tomato while highlighting the limitation of relying solely on a homology-based approach to predict interacting partners of F-box proteins.

Identifiants

pubmed: 38995464
doi: 10.1007/s11103-024-01483-4
pii: 10.1007/s11103-024-01483-4
doi:

Substances chimiques

F-Box Proteins 0
Plant Proteins 0
Phenylalanine Ammonia-Lyase EC 4.3.1.24
Acyltransferases EC 2.3.-
flavanone synthetase EC 2.3.1.74
Flavonoids 0
Propanols 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

85

Subventions

Organisme : National Science Foundation
ID : IOS-2142898
Organisme : National Institute of Food and Agriculture
ID : HATCH-7004334

Informations de copyright

© 2024. The Author(s), under exclusive licence to Springer Nature B.V.

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Auteurs

Doosan Shin (D)

Horticultural Sciences Department, University of Florida, Gainesville, FL, 32611, USA.

Keun Ho Cho (KH)

Horticultural Sciences Department, University of Florida, Gainesville, FL, 32611, USA.

Ethan Tucker (E)

Plant Molecular and Cellular Biology Graduate Program, University of Florida, Gainesville, FL, USA.

Chan Yul Yoo (CY)

School of Biological Sciences, University of Utah, Salt Lake City, UT, 84112, USA.

Jeongim Kim (J)

Horticultural Sciences Department, University of Florida, Gainesville, FL, 32611, USA. jkim6@ufl.edu.
Plant Molecular and Cellular Biology Graduate Program, University of Florida, Gainesville, FL, USA. jkim6@ufl.edu.

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