Article abstract
Nature Structural & Molecular Biology 14, 897 - 903 (2007)
Published online: 23 September 2007 | doi:10.1038/nsmb1302
A conserved motif in Argonaute-interacting proteins mediates functional interactions through the Argonaute PIWI domain
Susanne Till1,2, Erwan Lejeune1,2, Rolf Thermann1, Miriam Bortfeld1, Michael Hothorn1, Daniel Enderle1,3, Constanze Heinrich1,3, Matthias W Hentze1 & Andreas G Ladurner1
Abstract
Argonaute (Ago) proteins mediate silencing of nucleic acid targets by small RNAs. In fission yeast, Ago1, Tas3 and Chp1 assemble into a RITS complex, which silences transcription near centromeres. Here we describe a repetitive motif within Tas3, termed the 'Argonaute hook', that is conserved from yeast to humans and binds Ago proteins through their PIWI domains in vitro and in vivo. Site-directed mutation of key residues in the motif disrupts Ago binding and heterochromatic silencing in vivo. Unexpectedly, a PIWI domain pocket that binds the 5' end of the short interfering RNA guide strand is required for direct binding of the Ago hook. Moreover, wild-type but not mutant Ago hook peptides derepress microRNA-mediated translational silencing of a target messenger RNA. Proteins containing the conserved Ago hook may thus be important regulatory components of effector complexes in RNA interference.
- European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
- EMBL International PhD Programme.
- Present addresses: Center of Biosystems, Swiss Federal Institute of Technology Zürich, Mattenstrasse 26, 4058 Basel, Switzerland (D.E.); Friedrich Miescher Institute, Maulbeerstrasse 66, 4058 Basel, Switzerland (C.H.).
Correspondence to: Andreas G Ladurner1 e-mail: ladurner@embl.de
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