Ribosomal protein S3: a KH domain subunit in NF-kappaB complexes that mediates selective gene regulation.

NF-kappaB is a DNA-binding protein complex that transduces a variety of activating signals from the cytoplasm to specific sets of target genes. To understand the preferential recruitment of NF-kappaB to specific gene regulatory sites, we used NF-kappaB p65 in a tandem affinity purification and mass spectrometry proteomic screen. We identified ...
ribosomal protein S3 (RPS3), a KH domain protein, as a non-Rel subunit of p65 homodimer and p65-p50 heterodimer DNA-binding complexes that synergistically enhances DNA binding. RPS3 knockdown impaired NF-kappaB-mediated transcription of selected p65 target genes but not nuclear shuttling or global protein translation. Rather, lymphocyte-activating stimuli caused nuclear translocation of RPS3, parallel to p65, to form part of NF-kappaB bound to specific regulatory sites in chromatin. Thus, RPS3 is an essential but previously unknown subunit of NF-kappaB involved in the regulation of key genes in rapid cellular activation responses. Our observations provide insight into how NF-kappaB selectively controls gene expression.
Mesh Terms:
Active Transport, Cell Nucleus, Amino Acid Sequence, Cell Nucleus, Cells, Cultured, Chromatin, Gene Expression Regulation, Humans, Jurkat Cells, Molecular Sequence Data, Multiprotein Complexes, NF-kappa B, Protein Binding, Protein Structure, Tertiary, Protein Subunits, RNA, Small Interfering, Ribosomal Proteins, Substrate Specificity
Cell
Date: Nov. 30, 2007
Download Curated Data For This Publication
112613
Switch View:
  • Interactions 5