RPS3 enhances full-length NFκB-DNA binding through ternary complex formation

Abstract

Full-length NFκB (RelA-p50 heterodimer) is a transcription factor that responds to inflammatory and immune stress in human cells and is involved in cancer, inflammation, and autoimmune disorders. To better comprehend the control of the transcription of genes driven by NFκB, it is important to understand the roles played by other proteins in its kinetic regulation. Ribosomal Protein S3 (RPS3) is a protein component of the 40S subunit of the ribosome. It has been previously reported that NFκB gene expression is downregulated by RPS3 knockdown, indicating that NFκB has a dependence on RPS3.