IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v407y2000i6802d10.1038_35030169.html
   My bibliography  Save this article

Chromodomains are protein–RNA interaction modules

Author

Listed:
  • Asifa Akhtar

    (Adolf Butenandt-Institut, Molekularbiologie)

  • Daniele Zink

    (Institut für Anthropologie und Humangenetik, Ludwig-Maximilians-Universität)

  • Peter B. Becker

    (Adolf Butenandt-Institut, Molekularbiologie)

Abstract

In Drosophila, compensation for the reduced dosage of genes located on the single male X chromosome involves doubling their expression in relation to their counterparts on female X chromosomes1. Dosage compensation is an epigenetic process involving the specific acetylation of histone H4 at lysine 16 by the histone acetyltransferase MOF2,3,4,5. Although MOF is expressed in both sexes, it only associates with the X chromosome in males. Its absence causes male-specific lethality6. MOF is part of a chromosome-associated complex comprising male-specific lethal (MSL) proteins and at least one non-coding roX RNA7. How MOF is integrated into the dosage compensation complex is unknown. Here we show that association of MOF with the male X chromosome depends on its interaction with RNA. MOF specifically binds through its chromodomain to roX2 RNA in vivo. In vitro analyses of the MOF and MSL-3 chromodomains indicate that these chromodomains may function as RNA interaction modules. Their interaction with non-coding RNA may target regulators to specific chromosomal sites.

Suggested Citation

  • Asifa Akhtar & Daniele Zink & Peter B. Becker, 2000. "Chromodomains are protein–RNA interaction modules," Nature, Nature, vol. 407(6802), pages 405-409, September.
    • Handle: RePEc:nat:nature:v:407:y:2000:i:6802:d:10.1038_35030169
    DOI: 10.1038/35030169
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/35030169
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/35030169?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.

    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:407:y:2000:i:6802:d:10.1038_35030169. 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.