Search bioRxiv⌕ Search

Biology subjects

Yeh, G.

Publications and source records attributed to Yeh, G..

2 recordsLinked to original sources

Selective regulation of a defined subset of inflammatory and immunoregulatory genes by an NF-κB p50-IκBζ pathway

The five NF-{kappa}B family members and three nuclear I{kappa}B proteins play important biological roles, but the mechanisms by which distinct NF-{kappa}B and I{kappa}B proteins contribute to selective gene transcription remain poorly understood, especially at a genome-scale level. Using nascent transcript RNA-seq, we observed considerable overlap between p50-dependent and I{kappa}B{zeta}-dependent genes in Toll-like receptor 4 (TLR4)-activated macrophages. Key immunoregulatory genes, including Il6, Il1b, Nos2, Lcn2, and Batf, are among the p50-I{kappa}B{zeta} co-dependent genes. I{kappa}B{zeta} bound genomic sites occupied by NF-{kappa}B dimers at earlier time points. However, p50-I{kappa}B{zeta} co-dependence does not coincide with preferential binding of either p50 or I{kappa}B{zeta}, as both proteins and RelA co-occupy thousands of genomic sites. A common feature of p50-I{kappa}B{zeta} co-dependent genes is a nearby p50/RelA/I{kappa}B{zeta} co-bound site exhibiting p50-dependent binding of both RelA and I{kappa}B{zeta}. This result and others suggest that I{kappa}B{zeta} may act in concert with RelA:p50 heterodimers. Notably, the I{kappa}B{zeta}-dependent and p50-I{kappa}B{zeta}-co-dependent genes comprise a high percentage of genes that exhibit the greatest differential expression between TLR4-stimulated and tumor necrosis factor receptor (TNFR)-stimulated macrophages. Thus, our genome-centric analysis reveals a defined p50-I{kappa}B{zeta} pathway that selectively activates a set of key immunoregulatory genes and serves as an important contributor to the differential TNFR and TLR4 responses.

immunology↗

Stepwise neofunctionalization of the NF-κB family member c-Rel during vertebrate evolution

Adaptive immunity and the five vertebrate NF-{kappa}B/Rel family members first appeared in cartilaginous fish, suggesting that divergence and specialization within the NF-{kappa}B family helped facilitate the evolution of adaptive immunity. One specialized function of the NF-{kappa}B c-Rel protein in macrophages is the activation of Il12b, which encodes a key regulator of T-cell development. We found that c-Rel is a far more potent regulator of Il12b than of any other inducible genes in macrophages, with c-Rel regulation of Il12b dependent on its heightened intrinsic DNA-binding affinity. c-Rel homodimers regulate Il12b transcription in part via motifs with little resemblance to canonical NF-{kappa}B motifs. ChIP-seq experiments further defined distinct c-Rel DNA-binding preferences genome-wide, and X-ray crystallography of a c-Rel/RelA chimeric protein identified key amino acid changes that support the unique c-Rel properties. Unexpectedly, these changes, along with the c-Rel/RelA binding affinity differences, were largely restricted to mammalian species. Together, our findings reveal how a transcription factor family member can undergo a structural transition at a late stage of vertebrate evolution, resulting in an increased intrinsic DNA binding affinity and with clear functional consequences, presumably to support the increasing complexity of immune regulation.

immunology↗