N- and C-terminal non-conserved residues contribute to transactivation by a sea anemone (Nematostella vectensis) NF-κB transcription factor

Autor: Christine Pak, Dhishant Asarpota, Aditya Khedkar, Abishy Pandita, Ashley Ayers, Lauren Miller, Jingzhi Zhu, Shweta Kitchloo, Melissa Chua Ming Jie, Caitlin Lawlor, Fatema Abdurrob, Grace Thole, Sarah Heerboth, Majed Abbas, Jacob Bishop, Caryn Navarro, Anar Alshanbayeva, Janani Ramachandran, Mariam Maloyan, Alexis Aparicio, Yasmina Samaha, Neil A. Patel, Martine Tremblay, Nikhil Dhar, Alexa Diedrich, Isabel Park, Theresa Christie, Rosanna Hok, Marinaliz Reynoso, Shannon Linderman, Qianjing He, Brian Leonard, Linge Xia, Jason Turnbill, A. Aziz, Talal Almojel, Thomas D. Gilmore, Ajith Thomas, Chelsea L. Fortin, Oliver Chung
Rok vydání: 2015
Předmět:
Zdroj: BIOS. 86:165-175
ISSN: 1943-6289
0005-3155
DOI: 10.1893/0005-3155-86.4.165
Popis: 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 ...
Databáze: OpenAIRE