2. Academic Validation
  3. Identification of novel argonaute-associated proteins

Identification of novel argonaute-associated proteins

  • Curr Biol. 2005 Dec 6;15(23):2149-55. doi: 10.1016/j.cub.2005.10.048.
Gunter Meister 1,  Markus Landthaler,  Lasse Peters,  Po Yu Chen,  Henning Urlaub,  Reinhard Lührmann,  Thomas Tuschl
Affiliations

Affiliation

  • 1 Laboratory of RNA Molecular Biology, The Rockefeller University, 1230 York Avenue, Box 186, New York, New York 10021, USA. meister@biochem.mpg.de
PMID: 16289642 DOI: 10.1016/j.cub.2005.10.048
Abstract

RNA silencing processes are guided by small RNAs known as siRNAs and MicroRNAs (miRNAs) . They reside in ribonucleoprotein complexes, which guide the cleavage of complementary mRNAs or affect stability and translation of partial complementary mRNAs . Argonaute (Ago) proteins are at the heart of silencing effector complexes and bind the single-stranded siRNA and miRNA . Our biochemical analysis revealed that Ago2 is present in a pre-miRNA processing complex that is able to transfer the miRNA into a target-mRNA cleaving complex. To gain insight into the function and composition of RNA silencing complexes, we purified Ago1- and Ago2-containing complexes from human cells. Several known Ago1- and/or Ago2-associated proteins including Dicer were identified, but also two novel factors, the putative RNA helicase MOV10, and the RNA recognition motif (RRM)-containing protein TNRC6B/KIAA1093. The new proteins localize, similar to Ago proteins, to mRNA-degrading cytoplasmic P bodies, and they are functionally required to mediate miRNA-guided mRNA cleavage.

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