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. 2007 Nov 30;131(5):927-39.
doi: 10.1016/j.cell.2007.10.009.

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

Fengyi Wan  1 , D Eric Anderson, Robert A Barnitz, Andrew Snow, Nicolas Bidere, Lixin Zheng, Vijay Hegde, Lloyd T Lam, Louis M Staudt, David Levens, Walter A Deutsch, Michael J Lenardo
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Free article

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

Fengyi Wan et al. Cell. .
Free article

Abstract

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.

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