IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v443y2006i7107d10.1038_nature05080.html
   My bibliography  Save this article

Unravelling the dynamics of RNA degradation by ribonuclease II and its RNA-bound complex

Author

Listed:
  • Carlos Frazão

    (Division of Biological Chemistry)

  • Colin E. McVey

    (Division of Biological Chemistry)

  • Mónica Amblar

    (ITQB–Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Apt. 127)

  • Ana Barbas

    (ITQB–Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Apt. 127)

  • Clemens Vonrhein

    (Global Phasing Limited, Sheraton House, Castle Park)

  • Cecília M. Arraiano

    (ITQB–Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Apt. 127)

  • Maria A. Carrondo

    (Division of Biological Chemistry)

Abstract

Keeping RNA up to scratch RNA degradation by class II RNase family members plays a fundamental role in the maturation, turnover and quality control of RNA. The crystal structure of an RNase II has now been determined for the first time, in both RNA bound and ligand free forms. Surprisingly, the domain structure does not correspond to that predicted by sequence analysis. The molecule has two points of contact with the RNA: one site anchors the RNA, and the other catalyses cleavage. The structural details explain why RNase II acts only on single-stranded RNA, and how it moves along the RNA to processively degrade it.

Suggested Citation

  • Carlos Frazão & Colin E. McVey & Mónica Amblar & Ana Barbas & Clemens Vonrhein & Cecília M. Arraiano & Maria A. Carrondo, 2006. "Unravelling the dynamics of RNA degradation by ribonuclease II and its RNA-bound complex," Nature, Nature, vol. 443(7107), pages 110-114, September.
  • Handle: RePEc:nat:nature:v:443:y:2006:i:7107:d:10.1038_nature05080
    DOI: 10.1038/nature05080
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature05080
    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/nature05080?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. Zhiheng Yang & Wenzhe Liu & Lihua Zhao & Dongbao Yin & Jianfei Feng & Lidong Li & Xuefeng Guo, 2023. "Single-exonuclease nanocircuits reveal the RNA degradation dynamics of PNPase and demonstrate potential for RNA sequencing," Nature Communications, Nature, vol. 14(1), pages 1-14, 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:443:y:2006:i:7107:d:10.1038_nature05080. 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.