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Purification of maize nucleotide pyrophosphatase/phosphodiesterase casts doubt on the existence of zeatin cis–trans isomerase in plants

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F17%3A73584925" target="_blank" >RIV/61989592:15310/17:73584925 - isvavai.cz</a>

  • Result on the web

    <a href="https://www.frontiersin.org/articles/10.3389/fpls.2017.01473/full" target="_blank" >https://www.frontiersin.org/articles/10.3389/fpls.2017.01473/full</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3389/fpls.2017.01473" target="_blank" >10.3389/fpls.2017.01473</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Purification of maize nucleotide pyrophosphatase/phosphodiesterase casts doubt on the existence of zeatin cis–trans isomerase in plants

  • Original language description

    Almost 25 years ago, an enzyme named zeatin cis–trans isomerase from common bean has been described by Bassil et al. (1993). The partially purified enzyme required an external addition of FAD and dithiothreitol for the conversion of cis-zeatin to its trans- isomer that occurred only under light. Although an existence of this important enzyme involved in the metabolism of plant hormones cytokinins was generally accepted by plant biologists, the corresponding protein and encoding gene have not been identified to date. Based on the original paper, we purified and identified an enzyme from maize, which shows the described zeatin cis–trans isomerase activity. The enzyme belongs to nucleotide pyrophosphatase/phosphodiesterase family, which is well characterized in mammals, but less known in plants. Further experiments with the recombinant maize enzyme obtained from yeast expression system showed that rather than the catalytic activity of the enzyme itself, a non-enzymatic flavin induced photoisomerization is responsible for the observed zeatin cis–trans interconversion in vitro. An overexpression of the maize nucleotide pyrophosphatase/phosphodiesterase gene led to decreased FAD and increased FMN and riboflavin contents in transgenic Arabidopsis plants. However, neither contents nor the ratio of zeatin isomers was altered suggesting that the enzyme is unlikely to catalyze the interconversion of zeatin isomers in vivo. Using enhanced expression of a homologous gene, functional nucleotide pyrophosphatase/phosphodiesterase was also identified in rice.

  • 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

    10608 - Biochemistry and molecular biology

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

    2017

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Frontiers in Plant Science

  • ISSN

    1664-462X

  • e-ISSN

  • Volume of the periodical

    8

  • Issue of the periodical within the volume

    1473

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    13

  • Pages from-to

  • UT code for WoS article

    000408213200001

  • EID of the result in the Scopus database