Abstract
The extraribosomal functions of ribosomal proteins have drawn significant recent attention. Ribosomal protein S3 (RPS3), a component of the eukaryotic 40S ribosomal subunit, is a multifunctional protein that regulates DNA repair, apoptosis, and the innate immune response to bacterial infection. Here we the review the latest findings about RPS3 extraribosomal functions, with special emphasis on their relation to microbial pathogenesis and enteropathogenic Escherichia coli.
Highlights
Ribosomal proteins function in protein translation, and in multiple extraribosomal activities (Blumenthal and Carmichael, 1979)
We focus on a eukaryotic 40S ribosome component, the ribosomal protein S3 (RPS3), and its emerging regulatory roles in DNA repair, apoptosis, and pro-inflammatory signaling during bacterial infection
We propose that RPS3 may play a central role in regulating numerous aspects of host–pathogen interactions
Summary
Ribosomal proteins function in protein translation, and in multiple extraribosomal activities (Blumenthal and Carmichael, 1979). It was recently discovered that RPS3 is inducibly associated with and phosphorylated by IKKβ on serine 209 (S209) in response to NF-κB pathway activation (Wan et al, 2011). NF-κB binds to κB sites within target gene promoters and regulate transcription by recruiting co-activators/repressors (Wan et al, 2007). This newly discovered NF-κB subunit, RPS3, guides NF-κB to specific κB sites by increasing the affinity of the p65 NF-κB subunit for a subset of target gene promoters (Wan et al, 2007). NleH1, but not NleH2, inhibits the nuclear translocation of RPS3, inhibiting the transcription of genes encoding pro-inflammatory www.frontiersin.org
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