IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v415y2002i6875d10.1038_4151051a.html
   My bibliography  Save this article

Structure and dynamics of KH domains from FBP bound to single-stranded DNA

Author

Listed:
  • Demetrios T. Braddock

    (Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
    National Cancer Institute, National Institutes of Health)

  • John M. Louis

    (Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health)

  • James L. Baber

    (Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health)

  • David Levens

    (National Cancer Institute, National Institutes of Health)

  • G. Marius Clore

    (Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health)

Abstract

Gene regulation can be tightly controlled by recognition of DNA deformations that are induced by stress generated during transcription1,2,3. The KH domains of the FUSE-binding protein (FBP), a regulator of c-myc expression1,4, bind in vivo and in vitro to the single-stranded far-upstream element (FUSE), 1,500 base pairs upstream from the c-myc promoter4,5,6. FBP bound to FUSE acts through TFIIH at the promoter4. Here we report the solution structure of a complex between the KH3 and KH4 domains of FBP and a 29-base single-stranded DNA from FUSE. The KH domains recognize two sites, 9–10 bases in length, separated by 5 bases, with KH4 bound to the 5′ site and KH3 to the 3′ site. The central portion of each site comprises a tetrad of sequence 5′d-ATTC for KH4 and 5′d-TTTT for KH3. Dynamics measurements show that the two KH domains bind as articulated modules to single-stranded DNA, providing a flexible framework with which to recognize transient, moving targets.

Suggested Citation

  • Demetrios T. Braddock & John M. Louis & James L. Baber & David Levens & G. Marius Clore, 2002. "Structure and dynamics of KH domains from FBP bound to single-stranded DNA," Nature, Nature, vol. 415(6875), pages 1051-1056, February.
    • Handle: RePEc:nat:nature:v:415:y:2002:i:6875:d:10.1038_4151051a
    DOI: 10.1038/4151051a
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/4151051a
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/4151051a?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:415:y:2002:i:6875:d:10.1038_4151051a. 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.