Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells.
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.
Mesh Terms:
Carboxypeptidases, Cell Line, Eukaryotic Initiation Factor-2, Eukaryotic Initiation Factors, Gene Silencing, Genes, Reporter, Humans, Macromolecular Substances, MicroRNAs, Proteome, Proto-Oncogene Proteins, RNA, Messenger, RNA-Binding Proteins, Ribonuclease III, Ribonucleoproteins, ras Proteins
Carboxypeptidases, Cell Line, Eukaryotic Initiation Factor-2, Eukaryotic Initiation Factors, Gene Silencing, Genes, Reporter, Humans, Macromolecular Substances, MicroRNAs, Proteome, Proto-Oncogene Proteins, RNA, Messenger, RNA-Binding Proteins, Ribonuclease III, Ribonucleoproteins, ras Proteins
EMBO Rep.
Date: Nov. 01, 2007
PubMed ID: 17932509
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