Journal
CELL
Volume 131, Issue 5, Pages 927-939Publisher
CELL PRESS
DOI: 10.1016/j.cell.2007.10.009
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Funding
- Intramural NIH HHS Funding Source: Medline
- NCI NIH HHS [CA 109798] Funding Source: Medline
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NF-kappa B 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-kappa B to specific gene regulatory sites, we used NF-kappa B 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-kappa B-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-kappa B bound to specific regulatory sites in chromatin. Thus, RPS3 is an essential but previously unknown subunit of NF-kappa B involved in the regulation of key genes in rapid cellular activation responses. Our observations provide insight into how NF-kappa B selectively controls gene expression.
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