IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v416y2002i6876d10.1038_416038a.html
   My bibliography  Save this article

Plant desiccation gene found in a nematode

Author

Listed:
  • John Browne

    (National University of Ireland Maynooth)

  • Alan Tunnacliffe

    (Institute of Biotechnology, University of Cambridge)

  • Ann Burnell

    (National University of Ireland Maynooth)

Abstract

When subjected to drought conditions, some organisms enter a state of suspended animation known as anhydrobiosis1, surviving for indefinite periods until rehydration allows them to resume normal metabolism. We have identified a gene in the anhydrobiotic nematode Aphelenchus avenae that is upregulated in response to desiccation stress and whose encoded protein shares sequence similarity with a late-embryonic gene that is induced in many plants when they are deprived of water. This finding suggests that animals and plants that undergo anhydrobiosis may use common protective strategies against dehydration, and provides a unifying insight into the mechanism of anhydrobiosis.

Suggested Citation

  • John Browne & Alan Tunnacliffe & Ann Burnell, 2002. "Plant desiccation gene found in a nematode," Nature, Nature, vol. 416(6876), pages 38-38, March.
    • Handle: RePEc:nat:nature:v:416:y:2002:i:6876:d:10.1038_416038a
    DOI: 10.1038/416038a
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/416038a
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/416038a?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. Emmanuel Jaspard & Gilles Hunault, 2014. "Comparison of Amino Acids Physico-Chemical Properties and Usage of Late Embryogenesis Abundant Proteins, Hydrophilins and WHy Domain," PLOS ONE, Public Library of Science, vol. 9(10), pages 1-16, October.
    2. Rashmi Tripathi & Nathalie Benz & Bridget Culleton & Pascal Trouvé & Claude Férec, 2014. "Biophysical Characterisation of Calumenin as a Charged F508del-CFTR Folding Modulator," PLOS ONE, Public Library of Science, vol. 9(8), pages 1-15, August.

    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:416:y:2002:i:6876:d:10.1038_416038a. 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.