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Molecular and Cellular Biology, August 2009, p. 4144-4155, Vol. 29, No. 15
0270-7306/09/$08.00+0     doi:10.1128/MCB.00380-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Functional Dissection of the Human TNRC6 (GW182-Related) Family of Proteins {triangledown} ,{dagger}

David Baillat and Ramin Shiekhattar*

Gene Regulation Programme, Centre for Genomic Regulation, UPF, Barcelona, Spain, and Wistar Institute, 3601 Spruce Street, Philadelphia, Pennsylvania 19104

Received 24 March 2009/ Returned for modification 28 April 2009/ Accepted 15 May 2009

Argonaute (Ago) proteins through their association with small RNAs perform a critical function in the effector step of RNA interference. The TNRC6 (trinucleotide repeat containing 6) family of proteins have been shown to stably associate with Agos in mammalian cells. Here, we describe the isolation and functional characterization of TNRC6B- and TNRC6C-containing complexes. We show that TNRC6B and TNRC6C proteins associate with all four human Agos which are already loaded with microRNAs. Detailed domain analysis of TNRC6B protein indicated that distinct domains of the protein are required for Ago binding and P-body localization. Functional analysis using reporter constructs responsive to TNRC6B tethered through an MS2-binding domain indicates that neither the Ago-binding nor the P-body localization domains are required for translational silencing. In contrast, the C-terminal domain containing the RNA recognition motif plays a critical role in the silencing mediated by the TNRC6B protein.

* Corresponding author. Mailing address: Wistar Institute, 3601 Spruce Street, Philadelphia, PA 19104. Phone: (215) 898-3896. Fax: (215) 898-3986. E-mail: shiekhattar{at}wistar.org

{triangledown} Published ahead of print on 26 May 2009.

{dagger} Supplemental material for this article may be found at http://mcb.asm.org/.

Molecular and Cellular Biology, August 2009, p. 4144-4155, Vol. 29, No. 15
0270-7306/09/$08.00+0     doi:10.1128/MCB.00380-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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