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EMBO reports 8, 11, 1052–1060 (2007)
doi:10.1038/sj.embor.7401088
AOP Published online: 12 October 2007
Proteomic and functional analysis of Argonaute-containing mRNA–protein complexes in human cells
Julia Höck1, Lasse Weinmann1, Christine Ender1, Sabine Rüdel1, Elisabeth Kremmer2, Monika Raabe3, Henning Urlaub3 & Gunter Meister1
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1 Laboratory of RNA Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
2 GSF—Institute of Molecular Immunology, Marchioninistrasse 25, 81377 Munich, Germany
3 Bioanalytical Mass Spectrometry Group, Max Planck Institute of Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany
To whom correspondence should be addressed
Gunter Meister Tel: +49 89 8578 3420; Fax: +49 89 8578 3430; E-mail: meister@biochem.mpg.de
Received 18 May 2007; Accepted 5 September 2007; Published online 12 October 2007.
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Abstract
Members of the Argonaute (Ago) protein family associate with small RNAs and have important roles in RNA silencing. Here, we analysed Ago1- and Ago2-containing protein complexes in human cells. Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. A comprehensive proteomic analysis of Ago-containing mRNPs identified a large number of proteins involved in RNA metabolism. By using co-immunoprecipitation experiments followed by RNase treatment, we biochemically mapped interactions within Ago mRNPs. Using reporter assays and knockdown experiments, we showed that the putative RNA-binding protein RBM4 is required for microRNA-guided gene regulation.
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