• New protein discovery reveals the mechan

    From ScienceDaily@1:317/3 to All on Monday, April 11, 2022 22:30:34
    New protein discovery reveals the mechanisms of nitrogen assimilation in plants

    Date:
    April 11, 2022
    Source:
    Tohoku University
    Summary:
    Researchers recently discovered the protein inhibiting the
    formation of organic nitrogen compounds in plants. This protein,
    if manipulated, could potentially be used to encourage plant growth
    and improve crop harvests.



    FULL STORY ==========================================================================
    A collaborative research group has discovered the protein that inhibits
    the formation of organic nitrogen compounds in plants. This protein,
    if manipulated, could potentially be used to encourage plant growth,
    improving biomass production and crop harvests.


    ========================================================================== Nitrogen is one of the building blocks of life. Humans need nitrogen to
    make the amino acids, proteins, and nucleic acids essential for growth, hormones, brain functions, the immune system, and DNA and RNA. Humans,
    unlike plants, cannot synthesize organic nitrogen molecules. Instead,
    we rely on plants for our nitrogen intake.

    Plants utilise nitrate or ammonium in the environment to synthesize
    organic nitrogen molecules in a process called nitrogen assimilation. Crop production relies on nitrogen fertilizers to improve the efficiency
    of nitrogen uptake in crops. Still, the regulatory mechanisms behind
    nitrogen assimilation have continued to elude scientists.

    Multiple proteins mediate nitrogen assimilation. The expression of
    these proteins is high when the surrounding soil and water contains
    low amounts of ammonium and nitrate ions, suggesting the existence of
    a negative regulator dependent on these factors.

    Previous research by the group reported that the protein MYB1 serves a
    crucial role in inducing the expression of genes necessary for nitrogen assimilation, and it becomes inhibited in high nitrogen environments. The current findings revealed that the novel protein NDB1 inactivated
    MYB1. NDB1 traps MYB1 in the cytoplasm and prevents it from functioning
    as a transcription factor.

    "The NDB1-MYB1 pathway is a key factor in regulating nitrogen
    assimilation," says Kazuhiko Igarashi, professor at the Department of Biochemistry at Tohoku University's Graduate School of Medicine and
    co-author of the paper by Baifeng Zhou of the Institute of Innovative
    Research at Tokyo Institute of Technology.

    "Our discovery is a breakthrough for the field of plant science."
    The collaborative team led by Sousuke Imamura of the Institute of
    Innovative Research at Tokyo Institute of Technology also found that
    deleting the NDB1 gene enabled red alga to maintain the MYB1-dependent
    nitrate assimilation gene expression even in nitrogen-rich conditions, indicating that manipulating NDB1 can boost plant growth.

    Looking ahead, Igarashi is eager to explore the MYB1 transcription factor network further. "We would like to identify other proteins involved
    in regulating nitrogen assimilation and investigate whether nitrogen assimilation can be elevated through NDB1 manipulation."

    ========================================================================== Story Source: Materials provided by Tohoku_University. Note: Content
    may be edited for style and length.


    ========================================================================== Journal Reference:
    1. Baifeng Zhou, Hiroki Shima, Kazuhiko Igarashi, Kan Tanaka, Sousuke
    Imamura. CmNDB1 and a Specific Domain of CmMYB1 Negatively Regulate
    CmMYB1-Dependent Transcription of Nitrate Assimilation Genes Under
    Nitrogen-Repleted Condition in a Unicellular Red Alga. Frontiers
    in Plant Science, 2022; 13 DOI: 10.3389/fpls.2022.821947 ==========================================================================

    Link to news story: https://www.sciencedaily.com/releases/2022/04/220411101336.htm

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