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Yucasin is a potent inhibitor of YUCCA, a key enzyme in auxin biosynthesis.
Plant J. 2014 Feb; 77(3):352-66.PJ

Abstract

Indole-3-acetic acid (IAA), an auxin plant hormone, is biosynthesized from tryptophan. The indole-3-pyruvic acid (IPyA) pathway, involving the tryptophan aminotransferase TAA1 and YUCCA (YUC) enzymes, was recently found to be a major IAA biosynthetic pathway in Arabidopsis. TAA1 catalyzes the conversion of tryptophan to IPyA, and YUC produces IAA from IPyA. Using a chemical biology approach with maize coleoptiles, we identified 5-(4-chlorophenyl)-4H-1,2,4-triazole-3-thiol (yucasin) as a potent inhibitor of IAA biosynthesis in YUC-expressing coleoptile tips. Enzymatic analysis of recombinant AtYUC1-His suggested that yucasin strongly inhibited YUC1-His activity against the substrate IPyA in a competitive manner. Phenotypic analysis of Arabidopsis YUC1 over-expression lines (35S::YUC1) demonstrated that yucasin acts in IAA biosynthesis catalyzed by YUC. In addition, 35S::YUC1 seedlings showed resistance to yucasin in terms of root growth. A loss-of-function mutant of TAA1, sav3-2, was hypersensitive to yucasin in terms of root growth and hypocotyl elongation of etiolated seedlings. Yucasin combined with the TAA1 inhibitor l-kynurenine acted additively in Arabidopsis seedlings, producing a phenotype similar to yucasin-treated sav3-2 seedlings, indicating the importance of IAA biosynthesis via the IPyA pathway in root growth and leaf vascular development. The present study showed that yucasin is a potent inhibitor of YUC enzymes that offers an effective tool for analyzing the contribution of IAA biosynthesis via the IPyA pathway to plant development and physiological processes.

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Publisher Full Text (DOI)

Authors+Show Affiliations

Nishimura T
Department of Biological Sciences, Tokyo Metropolitan University, Hachioji-shi, Tokyo, 192-0397, Japan.
Hayashi K
No affiliation info available
Suzuki H
No affiliation info available
Gyohda A
No affiliation info available
Takaoka C
No affiliation info available
Sakaguchi Y
No affiliation info available
Matsumoto S
No affiliation info available
Kasahara H
No affiliation info available
Sakai T
No affiliation info available
Kato J
No affiliation info available
Kamiya Y
No affiliation info available
Koshiba T
No affiliation info available

MeSH

ArabidopsisArabidopsis ProteinsBiosynthetic PathwaysCotyledonDose-Response Relationship, DrugGene Expression Regulation, PlantIndoleacetic AcidsIndolesMutationOxygenasesPhenotypePlant Growth RegulatorsPlant LeavesPlant RootsPlant ShootsPlants, Genetically ModifiedRecombinant Fusion ProteinsSeedlingsSmall Molecule LibrariesTriazolesTryptophan TransaminaseZea mays

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

24299123

Citation

Nishimura, Takeshi, et al. "Yucasin Is a Potent Inhibitor of YUCCA, a Key Enzyme in Auxin Biosynthesis." The Plant Journal : for Cell and Molecular Biology, vol. 77, no. 3, 2014, pp. 352-66.
Nishimura T, Hayashi K, Suzuki H, et al. Yucasin is a potent inhibitor of YUCCA, a key enzyme in auxin biosynthesis. Plant J. 2014;77(3):352-66.
Nishimura, T., Hayashi, K., Suzuki, H., Gyohda, A., Takaoka, C., Sakaguchi, Y., Matsumoto, S., Kasahara, H., Sakai, T., Kato, J., Kamiya, Y., & Koshiba, T. (2014). Yucasin is a potent inhibitor of YUCCA, a key enzyme in auxin biosynthesis. The Plant Journal : for Cell and Molecular Biology, 77(3), 352-66. https://doi.org/10.1111/tpj.12399
Nishimura T, et al. Yucasin Is a Potent Inhibitor of YUCCA, a Key Enzyme in Auxin Biosynthesis. Plant J. 2014;77(3):352-66. PubMed PMID: 24299123.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Yucasin is a potent inhibitor of YUCCA, a key enzyme in auxin biosynthesis. AU - Nishimura,Takeshi, AU - Hayashi,Ken-Ichiro, AU - Suzuki,Hiromi, AU - Gyohda,Atsuko, AU - Takaoka,Chihiro, AU - Sakaguchi,Yusuke, AU - Matsumoto,Sachiko, AU - Kasahara,Hiroyuki, AU - Sakai,Tatsuya, AU - Kato,Jun-Ichi, AU - Kamiya,Yuji, AU - Koshiba,Tomokazu, Y1 - 2014/01/16/ PY - 2013/06/10/received PY - 2013/11/11/revised PY - 2013/11/19/accepted PY - 2013/12/5/entrez PY - 2013/12/5/pubmed PY - 2014/9/24/medline KW - Arabidopsis KW - IAA biosynthesis inhibitor KW - TAA KW - YUCCA KW - indole acetic acid KW - maize coleoptiles SP - 352 EP - 66 JF - The Plant journal : for cell and molecular biology JO - Plant J VL - 77 IS - 3 N2 - Indole-3-acetic acid (IAA), an auxin plant hormone, is biosynthesized from tryptophan. The indole-3-pyruvic acid (IPyA) pathway, involving the tryptophan aminotransferase TAA1 and YUCCA (YUC) enzymes, was recently found to be a major IAA biosynthetic pathway in Arabidopsis. TAA1 catalyzes the conversion of tryptophan to IPyA, and YUC produces IAA from IPyA. Using a chemical biology approach with maize coleoptiles, we identified 5-(4-chlorophenyl)-4H-1,2,4-triazole-3-thiol (yucasin) as a potent inhibitor of IAA biosynthesis in YUC-expressing coleoptile tips. Enzymatic analysis of recombinant AtYUC1-His suggested that yucasin strongly inhibited YUC1-His activity against the substrate IPyA in a competitive manner. Phenotypic analysis of Arabidopsis YUC1 over-expression lines (35S::YUC1) demonstrated that yucasin acts in IAA biosynthesis catalyzed by YUC. In addition, 35S::YUC1 seedlings showed resistance to yucasin in terms of root growth. A loss-of-function mutant of TAA1, sav3-2, was hypersensitive to yucasin in terms of root growth and hypocotyl elongation of etiolated seedlings. Yucasin combined with the TAA1 inhibitor l-kynurenine acted additively in Arabidopsis seedlings, producing a phenotype similar to yucasin-treated sav3-2 seedlings, indicating the importance of IAA biosynthesis via the IPyA pathway in root growth and leaf vascular development. The present study showed that yucasin is a potent inhibitor of YUC enzymes that offers an effective tool for analyzing the contribution of IAA biosynthesis via the IPyA pathway to plant development and physiological processes. SN - 1365-313X UR - https://www.unboundmedicine.com/medline/citation/24299123/Yucasin_is_a_potent_inhibitor_of_YUCCA_a_key_enzyme_in_auxin_biosynthesis_ DB - PRIME DP - Unbound Medicine ER -