IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v13y2022i1d10.1038_s41467-022-29275-8.html
   My bibliography  Save this article

Mechanistic insights into the regulation of plant phosphate homeostasis by the rice SPX2 – PHR2 complex

Author

Listed:
  • Zeyuan Guan

    (Huazhong Agricultural University)

  • Qunxia Zhang

    (Huazhong Agricultural University)

  • Zhifei Zhang

    (Huazhong Agricultural University)

  • Jiaqi Zuo

    (Huazhong Agricultural University)

  • Juan Chen

    (Huazhong Agricultural University)

  • Ruiwen Liu

    (Huazhong Agricultural University)

  • Julie Savarin

    (University of Geneva)

  • Larissa Broger

    (University of Geneva)

  • Peng Cheng

    (Huazhong Agricultural University)

  • Qiang Wang

    (Huazhong Agricultural University)

  • Kai Pei

    (Huazhong Agricultural University)

  • Delin Zhang

    (Huazhong Agricultural University)

  • Tingting Zou

    (Huazhong Agricultural University)

  • Junjie Yan

    (Huazhong Agricultural University)

  • Ping Yin

    (Huazhong Agricultural University)

  • Michael Hothorn

    (University of Geneva)

  • Zhu Liu

    (Huazhong Agricultural University)

Abstract

Phosphate (Pi) starvation response (PHR) transcription factors play key roles in plant Pi homeostasis maintenance. They are negatively regulated by stand-alone SPX proteins, cellular receptors for inositol pyrophosphate (PP-InsP) nutrient messengers. How PP-InsP-bound SPX interacts with PHRs is poorly understood. Here, we report crystal structures of the rice SPX2/InsP6/PHR2 complex and of the PHR2 DNA binding (MYB) domain in complex with target DNA at resolutions of 3.1 Å and 2.7 Å, respectively. In the SPX2/InsP6/PHR2 complex, the signalling-active SPX2 assembles into a domain-swapped dimer conformation and binds two copies of PHR2, targeting both its coiled-coil (CC) oligomerisation domain and MYB domain. Our results reveal that the SPX2 senses PP-InsPs to inactivate PHR2 by establishing severe steric clashes with the PHR2 MYB domain, preventing DNA binding, and by disrupting oligomerisation of the PHR2 CC domain, attenuating promoter binding. Our findings rationalize how PP-InsPs activate SPX receptor proteins to target PHR family transcription factors.

Suggested Citation

  • Zeyuan Guan & Qunxia Zhang & Zhifei Zhang & Jiaqi Zuo & Juan Chen & Ruiwen Liu & Julie Savarin & Larissa Broger & Peng Cheng & Qiang Wang & Kai Pei & Delin Zhang & Tingting Zou & Junjie Yan & Ping Yin, 2022. "Mechanistic insights into the regulation of plant phosphate homeostasis by the rice SPX2 – PHR2 complex," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-29275-8
    DOI: 10.1038/s41467-022-29275-8
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-022-29275-8
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-022-29275-8?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    References listed on IDEAS

    as
    1. Jia Zhou & Qinli Hu & Xinlong Xiao & Deqiang Yao & Shenghong Ge & Jin Ye & Haojie Li & Rujie Cai & Renyang Liu & Fangang Meng & Chao Wang & Jian-Kang Zhu & Mingguang Lei & Weiman Xing, 2021. "Mechanism of phosphate sensing and signaling revealed by rice SPX1-PHR2 complex structure," Nature Communications, Nature, vol. 12(1), pages 1-10, December.
    2. Martina K. Ried & Rebekka Wild & Jinsheng Zhu & Joka Pipercevic & Kristina Sturm & Larissa Broger & Robert K. Harmel & Luciano A. Abriata & Ludwig A. Hothorn & Dorothea Fiedler & Sebastian Hiller & Mi, 2021. "Inositol pyrophosphates promote the interaction of SPX domains with the coiled-coil motif of PHR transcription factors to regulate plant phosphate homeostasis," Nature Communications, Nature, vol. 12(1), pages 1-13, December.
    Full references (including those not matched with items on IDEAS)

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Zeyuan Guan & Juan Chen & Ruiwen Liu & Yanke Chen & Qiong Xing & Zhangmeng Du & Meng Cheng & Jianjian Hu & Wenhui Zhang & Wencong Mei & Beijing Wan & Qiang Wang & Jie Zhang & Peng Cheng & Huanyu Cai &, 2023. "The cytoplasmic synthesis and coupled membrane translocation of eukaryotic polyphosphate by signal-activated VTC complex," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    2. Yukari Nagatoshi & Kenta Ikazaki & Yasufumi Kobayashi & Nobuyuki Mizuno & Ryohei Sugita & Yumiko Takebayashi & Mikiko Kojima & Hitoshi Sakakibara & Natsuko I. Kobayashi & Keitaro Tanoi & Kenichiro Fuj, 2023. "Phosphate starvation response precedes abscisic acid response under progressive mild drought in plants," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.
    1. Yukari Nagatoshi & Kenta Ikazaki & Yasufumi Kobayashi & Nobuyuki Mizuno & Ryohei Sugita & Yumiko Takebayashi & Mikiko Kojima & Hitoshi Sakakibara & Natsuko I. Kobayashi & Keitaro Tanoi & Kenichiro Fuj, 2023. "Phosphate starvation response precedes abscisic acid response under progressive mild drought in plants," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    2. Jia Zhou & Qinli Hu & Xinlong Xiao & Deqiang Yao & Shenghong Ge & Jin Ye & Haojie Li & Rujie Cai & Renyang Liu & Fangang Meng & Chao Wang & Jian-Kang Zhu & Mingguang Lei & Weiman Xing, 2021. "Mechanism of phosphate sensing and signaling revealed by rice SPX1-PHR2 complex structure," Nature Communications, Nature, vol. 12(1), pages 1-10, December.
    3. Joka Pipercevic & Bastian Kohl & Ruta Gerasimaite & Véronique Comte-Miserez & Sarah Hostachy & Thomas Müntener & Elia Agustoni & Henning Jacob Jessen & Dorothea Fiedler & Andreas Mayer & Sebastian Hil, 2023. "Inositol pyrophosphates activate the vacuolar transport chaperone complex in yeast by disrupting a homotypic SPX domain interaction," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    4. Zeyuan Guan & Juan Chen & Ruiwen Liu & Yanke Chen & Qiong Xing & Zhangmeng Du & Meng Cheng & Jianjian Hu & Wenhui Zhang & Wencong Mei & Beijing Wan & Qiang Wang & Jie Zhang & Peng Cheng & Huanyu Cai &, 2023. "The cytoplasmic synthesis and coupled membrane translocation of eukaryotic polyphosphate by signal-activated VTC complex," Nature Communications, Nature, vol. 14(1), pages 1-12, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-29275-8. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.