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• W2279227835 startingPage "165" @default.
• W2279227835 abstract "NF-κB is an evolutionarily conserved eukaryotic transcription factor that plays a role in many important developmental and immune-related processes by activating target gene expression. The goal of these experiments was to define the sequences required for a sea anemone NF-κB's intrinsic transactivation activity by using mutant proteins with serial deletions of the N- and C-terminal sequences. Deletion mutants were constructed that were missing the C-terminal 15, 32 or 47 amino acids (aa) or the N-terminal 17, 27 or 47 aa of the 440 aa NF-κB protein from the starlet sea anemone, Nematostella vectensis (Nv), a simple model organism in the phylum Cnidaria. These Nv-NF-κB mutants were expressed as GAL4 fusion proteins in yeast, and their transactivation activities were assessed by LacZ reporter gene assays. The deletion of 47 aa from either the N terminus or the C terminus of NF-κB completely inactivates the transactivation function of Nv-NF-κB. In addition, we identified proline-258 in the center of the protein as a key residue for the transactivation function of Nv-NF-κB. Taken together, these results demonstrate that non-conserved N- and C-terminal residues are both required for the transcriptional activating function of the sea anemone NF-κB protein, suggesting that it has a novel functional domain structure among known NF-κB proteins." @default.
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• W2279227835 date "2015-12-01" @default.
• W2279227835 modified "2023-09-27" @default.
• W2279227835 title "N- and C-terminal non-conserved residues contribute to transactivation by a sea anemone (Nematostella vectensis) NF-κB transcription factor" @default.
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• W2279227835 doi "https://doi.org/10.1893/0005-3155-86.4.165" @default.
• W2279227835 hasPublicationYear "2015" @default.
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