IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v448y2007i7154d10.1038_nature05960.html
   My bibliography  Save this article

JAZ repressor proteins are targets of the SCFCOI1 complex during jasmonate signalling

Author

Listed:
  • Bryan Thines

    (Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340, USA
    Present address: USDA Plant Gene Expression Center, 800 Buchanan Street, Albany, California 94710, USA.)

  • Leron Katsir

    (Department of Energy-Plant Research Laboratory,
    Department of Biochemistry and Molecular Biology,)

  • Maeli Melotto

    (Department of Energy-Plant Research Laboratory,)

  • Yajie Niu

    (Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340, USA)

  • Ajin Mandaokar

    (Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340, USA)

  • Guanghui Liu

    (Department of Energy-Plant Research Laboratory,)

  • Kinya Nomura

    (Department of Energy-Plant Research Laboratory,)

  • Sheng Yang He

    (Department of Energy-Plant Research Laboratory,
    Michigan State University, East Lansing, Michigan 48824, USA)

  • Gregg A. Howe

    (Department of Energy-Plant Research Laboratory,
    Department of Biochemistry and Molecular Biology,)

  • John Browse

    (Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340, USA)

Abstract

Jasmonate and related signalling compounds have a crucial role in both host immunity and development in plants, but the molecular details of the signalling mechanism are poorly understood. Here we identify members of the jasmonate ZIM-domain (JAZ) protein family as key regulators of jasmonate signalling. JAZ1 protein acts to repress transcription of jasmonate-responsive genes. Jasmonate treatment causes JAZ1 degradation and this degradation is dependent on activities of the SCFCOI1 ubiquitin ligase and the 26S proteasome. Furthermore, the jasmonoyl–isoleucine (JA–Ile) conjugate, but not other jasmonate-derivatives such as jasmonate, 12-oxo-phytodienoic acid, or methyl-jasmonate, promotes physical interaction between COI1 and JAZ1 proteins in the absence of other plant proteins. Our results suggest a model in which jasmonate ligands promote the binding of the SCFCOI1 ubiquitin ligase to and subsequent degradation of the JAZ1 repressor protein, and implicate the SCFCOI1–JAZ1 protein complex as a site of perception of the plant hormone JA–Ile.

Suggested Citation

  • Bryan Thines & Leron Katsir & Maeli Melotto & Yajie Niu & Ajin Mandaokar & Guanghui Liu & Kinya Nomura & Sheng Yang He & Gregg A. Howe & John Browse, 2007. "JAZ repressor proteins are targets of the SCFCOI1 complex during jasmonate signalling," Nature, Nature, vol. 448(7154), pages 661-665, August.
  • Handle: RePEc:nat:nature:v:448:y:2007:i:7154:d:10.1038_nature05960
    DOI: 10.1038/nature05960
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature05960
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.

    File URL: https://libkey.io/10.1038/nature05960?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
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

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


    Cited by:

    1. Yao Xia & Rongfeng Zou & Maxime Escouboué & Liang Zhong & Chengjun Zhu & Cécile Pouzet & Xueqiang Wu & Yongjin Wang & Guohua Lv & Haibo Zhou & Pinghua Sun & Ke Ding & Laurent Deslandes & Shuguang Yuan, 2021. "Secondary-structure switch regulates the substrate binding of a YopJ family acetyltransferase," Nature Communications, Nature, vol. 12(1), pages 1-10, December.
    2. Xiaoyue Chen & Graham A. Hudson & Charlotte Mineo & Bashar Amer & Edward E. K. Baidoo & Samantha A. Crowe & Yuzhong Liu & Jay D. Keasling & Henrik V. Scheller, 2023. "Deciphering triterpenoid saponin biosynthesis by leveraging transcriptome response to methyl jasmonate elicitation in Saponaria vaccaria," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    3. Ameneh Asadi-Sardari & Esmat Mahdikhani-Moghadam & Mohammad Zaki-Aghl & Ramesh Raju Vetukuri, 2022. "Constitutive and Inducible Expression of Genes Related to Salicylic Acid and Ethylene Pathways in a Moderately Resistant Tomato Cultivar Leads to Delayed Development of Meloidogyne javanica," Agriculture, MDPI, vol. 12(12), pages 1-22, December.
    4. Zi-Wei Yan & Fang-Yan Chen & Xian Zhang & Wen-Juan Cai & Chun-Yu Chen & Jie Liu & Man-Ni Wu & Ning-Jing Liu & Bin Ma & Mu-Yang Wang & Dai-Yin Chao & Cai-Ji Gao & Ying-Bo Mao, 2023. "Endocytosis-mediated entry of a caterpillar effector into plants is countered by Jasmonate," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    5. Jinping Zou & Xinlin Chen & Chenxu Liu & Mingyue Guo & Mukesh Kumar Kanwar & Zhenyu Qi & Ping Yang & Guanghui Wang & Yan Bao & Diane C. Bassham & Jingquan Yu & Jie Zhou, 2023. "Autophagy promotes jasmonate-mediated defense against nematodes," Nature Communications, Nature, vol. 14(1), pages 1-16, 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:nature:v:448:y:2007:i:7154:d:10.1038_nature05960. 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.

    We have no bibliographic references for this item. You can help adding them by using 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.