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Dioxygenase for auxin oxidation 1 catalyzes the oxidation of IAA amino acid conjugates

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389030%3A_____%2F21%3A00551736" target="_blank" >RIV/61389030:_____/21:00551736 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216208:11310/21:10432705 RIV/61989592:15310/21:73610708

  • Result on the web

    <a href="http://doi.org/10.1093/plphys/kiab242" target="_blank" >http://doi.org/10.1093/plphys/kiab242</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1093/plphys/kiab242" target="_blank" >10.1093/plphys/kiab242</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Dioxygenase for auxin oxidation 1 catalyzes the oxidation of IAA amino acid conjugates

  • Original language description

    Together with auxin transport, auxin metabolism is a key determinant of auxin signaling output by plant cells. Enzymatic machinery involved in auxin metabolism is subject to regulation based on numerous inputs, including the concentration of auxin itself. Therefore, experiments characterizing altered auxin availability and subsequent changes in auxin metabolism could elucidate the function and regulatory role of individual elements in the auxin metabolic machinery. Here, we studied auxin metabolism in auxin-dependent tobacco BY-2 cells. We revealed that the concentration of N-(2-oxindole-3-acetyl)-L-aspartic acid (oxIAA-Asp), the most abundant auxin metabolite produced in the control culture, dramatically decreased in auxin-starved BY-2 cells. Analysis of the transcriptome and proteome in auxin-starved cells uncovered significant downregulation of all tobacco (Nicotiana tabacum) homologs of Arabidopsis (Arabidopsis thaliana) DIOXYGENASE FOR AUXIN OXIDATION 1 (DAO1), at both transcript and protein levels. Auxin metabolism profiling in BY-2 mutants carrying either siRNA-silenced or CRISPR-Cas9-mutated NtDAO1, as well as in dao1-1 Arabidopsis plants, showed not only the expected lower levels of oxIAA, but also significantly lower abundance of oxIAA-Asp. Finally, ability of DAO1 to oxidize IAA-Asp was confirmed by an enzyme assay in AtDAO1-producing bacterial culture. Our results thus represent direct evidence of DAO1 activity on IAA amino acid conjugates.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10611 - Plant sciences, botany

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2021

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Plant Physiology

  • ISSN

    0032-0889

  • e-ISSN

    1532-2548

  • Volume of the periodical

    187

  • Issue of the periodical within the volume

    1

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    13

  • Pages from-to

    103-115

  • UT code for WoS article

    000696244400019

  • EID of the result in the Scopus database

    2-s2.0-85114456402