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January 22nd, 2025
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Boston University
molecular biology
biorxiv

Comparison of Activities of Transcription Factor NF-κB from Two Jellyfish Models

Williams, L. M.Open in Google Scholar•Wang, W.Open in Google Scholar•Grigoryeva, A. V.Open in Google Scholar•Navarro-Rosado, A.Open in Google Scholar•Peart, J. A.Open in Google Scholar•Calderon, A.Open in Google Scholar•Gill, C. L.Open in Google Scholar•Alsante, K. M.Open in Google Scholar•Lackstrom, A. T.Open in Google Scholar•Molecular Biology Laboratory,Open in Google Scholaret al.

Herein, transcription factor NF-{kappa}B is characterized from two model jellyfish, Aurelia aurita (Aa) and Clytia hemisphaerica (Ch). Both jellyfish NF-{kappa}B proteins consist primarily of the N-terminal DNA-binding/dimerization domain, and they lack the C-terminal ankyrin repeat inhibitory domain found in vertebrate NF-{kappa}B proteins. Both jellyfish NF-{kappa}B proteins can bind to a consensus mammalian NF-{kappa}B binding site, and their AlphaFold3-predicted structures on DNA are similar to that of mouse NF-{kappa}B p50. Neither Aa- nor Ch-NF-{kappa}B activated transcription of an NF-{kappa}B-site reporter gene in human cells; however, Aa-NF-{kappa}B did activate transcription from a GAL4-site reporter gene in yeast, whereas Ch-NF-{kappa}B did not. Aa- and Ch-NF-{kappa}B were both constitutively located in the nucleus when expressed in vertebrate cells. Homologs of I{kappa}B-like proteins from both species interacted with their corresponding NF-{kappa}B proteins in co-immunoprecipitation assays in HEK 293T cells. These I{kappa}B-like proteins influenced the subcellular localization of their cognate NF-{kappa}B proteins in vertebrate cells, and their ankyrin repeat domains were predicted to interact with Ch-NF-{kappa}B in a manner similar to mammalian I{kappa}B and NF-{kappa}B. RNA-sequencing data from Ch animals indicate that Ch-NF-{kappa}B is expressed at high levels in early developmental stages, when Ch-I{kappa}B expression is low, suggesting that active Ch-NF-{kappa}B controls an early developmental process. In contrast, in adult animals the expression of Ch-I{kappa}B is high, suggesting that Ch-NF-{kappa}B requires a signal in order to become active. Overall, these results provide comparative information on the structure, activity, and mRNA expression of jellyfish NF-{kappa}B pathway proteins among jellyfish, and they suggest roles for NF-{kappa}B in developing and adult jellyfish.

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