Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Brief Communication
  • Published:

Nucleic acid 3′-end recognition by the Argonaute2 PAZ domain

Nature Structural & Molecular Biology volume 11, pages 576–577 (2004)Cite this article

Abstract

We describe the solution structures of the Argonaute2 PAZ domain bound to RNA and DNA oligonucleotides. The structures reveal a unique mode of single-stranded nucleic acid binding in which the two 3′-terminal nucleotides are buried in a hydrophobic cleft. We propose that the PAZ domain contributes to the specific recognition of siRNAs by providing a binding pocket for their characteristic two-nucleotide 3′ overhangs.

This is a preview of subscription content, access via your institution

Access options

Buy this article

  • Purchase on SpringerLink
  • Instant access to full article PDF
Buy now

Prices may be subject to local taxes which are calculated during checkout

Figure 1: Structure of the Ago2 PAZ domain bound to a pentamer DNA or RNA oligonucleotide.
Figure 2: Details of nucleic acid recognition.

Similar content being viewed by others

Accession codes

Accessions

Protein Data Bank

References

  1. Hammond, S.M., Boettcher, S., Caudy, A.A., Kobayashi, R. & Hannon, G.J. Science 293, 1146–1150 (2001).

    Article  CAS  Google Scholar 

  2. Cerutti, L., Mian, N. & Bateman, A. Trends Biochem. Sci. 25, 481–482 (2000).

    Article  CAS  Google Scholar 

  3. Carmell, M.A., Xuan, Z., Zhang, M.Q. & Hannon, G.J. Genes Dev. 16, 2733–2742 (2002).

    Article  CAS  Google Scholar 

  4. Yan, K.S. et al. Nature 426, 468–474 (2003).

    Article  Google Scholar 

  5. Lingel, A., Simon, B., Izaurralde, E. & Sattler, M. Nature 426, 465–469 (2003).

    Article  CAS  Google Scholar 

  6. Song, J.J. et al. Nat. Struct. Mol. Biol. 10, 1026–1032 (2003).

    Article  CAS  Google Scholar 

Download references

Acknowledgements

We thank G. Stier and S. Bäckström for the pETM60 vector, M. Nilges for discussions, H. Siomi for the Ago2 cDNA, the Center for Biomolecular Magnetic Resonance (BMRZ) in Frankfurt for NMR measurement time, and Biospring (Frankfurt) for RNA synthesis. This study was supported by the European Molecular Biology Organization, the German Research Foundation, the European Union and the Human Frontier Science Program Organization.

Author information

Authors and Affiliations

  1. European Molecular Biology Laboratory, Meyerhofstrasse 1, Heidelberg, D-69117, Germany

    Andreas Lingel, Bernd Simon, Elisa Izaurralde & Michael Sattler

Authors
  1. Andreas Lingel
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Bernd Simon
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Elisa Izaurralde
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Michael Sattler
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding authors

Correspondence to Elisa Izaurralde or Michael Sattler.

Ethics declarations

Competing interests

The authors declare no competing financial interests.

Supplementary information

Rights and permissions

Reprints and permissions

About this article

Cite this article

Lingel, A., Simon, B., Izaurralde, E. et al. Nucleic acid 3′-end recognition by the Argonaute2 PAZ domain. Nat Struct Mol Biol 11, 576–577 (2004). https://doi.org/10.1038/nsmb777

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1038/nsmb777

This article is cited by

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing