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Indole-3-pyruvic acid regulates TAA1 activity, which plays a key role in coordinating the two steps of auxin biosynthesis
Auxin biosynthesis involves two types of enzymes: the Trp aminotransferases (TAA/TARs) and the flavin monooxygenases (YUCCAs). This two-step pathway is highly conserved throughout the plant kingdom and is essential for almost all of the major developmental processes. Despite their importance, it is...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
National Academy of Sciences
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9231625/ https://www.ncbi.nlm.nih.gov/pubmed/35696560 http://dx.doi.org/10.1073/pnas.2203633119 |
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author | Sato, Akiko Soeno, Kazuo Kikuchi, Rie Narukawa-Nara, Megumi Yamazaki, Chiaki Kakei, Yusuke Nakamura, Ayako Shimada, Yukihisa |
author_facet | Sato, Akiko Soeno, Kazuo Kikuchi, Rie Narukawa-Nara, Megumi Yamazaki, Chiaki Kakei, Yusuke Nakamura, Ayako Shimada, Yukihisa |
author_sort | Sato, Akiko |
collection | PubMed |
description | Auxin biosynthesis involves two types of enzymes: the Trp aminotransferases (TAA/TARs) and the flavin monooxygenases (YUCCAs). This two-step pathway is highly conserved throughout the plant kingdom and is essential for almost all of the major developmental processes. Despite their importance, it is unclear how these enzymes are regulated and how their activities are coordinated. Here, we show that TAA1/TARs are regulated by their product indole-3-pyruvic acid (IPyA) (or its mimic KOK2099) via negative feedback regulation in Arabidopsis thaliana. This regulatory system also functions in rice and tomato. This negative feedback regulation appears to be achieved by both the reversibility of Trp aminotransferase activity and the competitive inhibition of TAA1 activity by IPyA. The K(m) value of IPyA is 0.7 µM, and that of Trp is 43.6 µM; this allows IPyA to be maintained at low levels and prevents unfavorable nonenzymatic indole-3-acetic acid (IAA) formation from IPyA in vivo. Thus, IPyA levels are maintained by the push (by TAA1/TARs) and pull (by YUCCAs) of the two biosynthetic enzymes, in which TAA1 plays a key role in preventing the over- or under-accumulation of IPyA. TAA1 prefer Ala among various amino acid substrates in the reverse reaction of auxin biosynthesis, allowing TAA1 to show specificity for converting Trp and pyruvate to IPyA and Ala, and the reverse reaction. |
format | Online Article Text |
id | pubmed-9231625 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | National Academy of Sciences |
record_format | MEDLINE/PubMed |
spelling | pubmed-92316252022-12-13 Indole-3-pyruvic acid regulates TAA1 activity, which plays a key role in coordinating the two steps of auxin biosynthesis Sato, Akiko Soeno, Kazuo Kikuchi, Rie Narukawa-Nara, Megumi Yamazaki, Chiaki Kakei, Yusuke Nakamura, Ayako Shimada, Yukihisa Proc Natl Acad Sci U S A Biological Sciences Auxin biosynthesis involves two types of enzymes: the Trp aminotransferases (TAA/TARs) and the flavin monooxygenases (YUCCAs). This two-step pathway is highly conserved throughout the plant kingdom and is essential for almost all of the major developmental processes. Despite their importance, it is unclear how these enzymes are regulated and how their activities are coordinated. Here, we show that TAA1/TARs are regulated by their product indole-3-pyruvic acid (IPyA) (or its mimic KOK2099) via negative feedback regulation in Arabidopsis thaliana. This regulatory system also functions in rice and tomato. This negative feedback regulation appears to be achieved by both the reversibility of Trp aminotransferase activity and the competitive inhibition of TAA1 activity by IPyA. The K(m) value of IPyA is 0.7 µM, and that of Trp is 43.6 µM; this allows IPyA to be maintained at low levels and prevents unfavorable nonenzymatic indole-3-acetic acid (IAA) formation from IPyA in vivo. Thus, IPyA levels are maintained by the push (by TAA1/TARs) and pull (by YUCCAs) of the two biosynthetic enzymes, in which TAA1 plays a key role in preventing the over- or under-accumulation of IPyA. TAA1 prefer Ala among various amino acid substrates in the reverse reaction of auxin biosynthesis, allowing TAA1 to show specificity for converting Trp and pyruvate to IPyA and Ala, and the reverse reaction. National Academy of Sciences 2022-06-13 2022-06-21 /pmc/articles/PMC9231625/ /pubmed/35696560 http://dx.doi.org/10.1073/pnas.2203633119 Text en Copyright © 2022 the Author(s). Published by PNAS. https://creativecommons.org/licenses/by-nc-nd/4.0/This article is distributed under Creative Commons Attribution-NonCommercial-NoDerivatives License 4.0 (CC BY-NC-ND) (https://creativecommons.org/licenses/by-nc-nd/4.0/) . |
spellingShingle | Biological Sciences Sato, Akiko Soeno, Kazuo Kikuchi, Rie Narukawa-Nara, Megumi Yamazaki, Chiaki Kakei, Yusuke Nakamura, Ayako Shimada, Yukihisa Indole-3-pyruvic acid regulates TAA1 activity, which plays a key role in coordinating the two steps of auxin biosynthesis |
title | Indole-3-pyruvic acid regulates TAA1 activity, which plays a key role in coordinating the two steps of auxin biosynthesis |
title_full | Indole-3-pyruvic acid regulates TAA1 activity, which plays a key role in coordinating the two steps of auxin biosynthesis |
title_fullStr | Indole-3-pyruvic acid regulates TAA1 activity, which plays a key role in coordinating the two steps of auxin biosynthesis |
title_full_unstemmed | Indole-3-pyruvic acid regulates TAA1 activity, which plays a key role in coordinating the two steps of auxin biosynthesis |
title_short | Indole-3-pyruvic acid regulates TAA1 activity, which plays a key role in coordinating the two steps of auxin biosynthesis |
title_sort | indole-3-pyruvic acid regulates taa1 activity, which plays a key role in coordinating the two steps of auxin biosynthesis |
topic | Biological Sciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9231625/ https://www.ncbi.nlm.nih.gov/pubmed/35696560 http://dx.doi.org/10.1073/pnas.2203633119 |
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