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Despite the important role of the antizyme-AZIN protein-protein interaction (PPI) in cell cycle regulation, there are no assays for directly measuring the binding of AZIN to antizyme that are amenable to high throughput screening. To address this problem, we developed and validated a novel antizyme-AZIN intramolecular FRET sensor using clover and mRuby2 fluorescent proteins. By introducing alanine mutations in the AZIN protein, we used this sensor to probe the PPI for key residues governing the binding interaction. We found that like many PPIs, the energy of the antizyme-AZIN binding interaction is distributed across many amino acid residues; mutation of individual residues did not have a significant effect on disrupting the PPI. We also examined the interaction between Clover-AZIN and antizyme-mRuby2 in cells. Evidence of a direct interaction between Clover-AZIN and antizyme-mRuby2 was observed within cells, validating the use of this FRET sensor for probing intracellular antizyme-AZIN PPI. In conclusion, we have developed and optimized a FRET sensor which can be adapted for high throughput screening of either <jats:italic>in vitro<\/jats:italic> or intracellular activity.<\/jats:p>","DOI":"10.1038\/s41598-019-40929-4","type":"journal-article","created":{"date-parts":[[2019,3,15]],"date-time":"2019-03-15T11:02:32Z","timestamp":1552647752000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["Developing a novel FRET assay, targeting the binding between Antizyme-AZIN"],"prefix":"10.1038","volume":"9","author":[{"given":"Aram","family":"Ghalali","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James M.","family":"Rice","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Amanda","family":"Kusztos","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Finith E.","family":"Jernigan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bruce R.","family":"Zetter","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael S.","family":"Rogers","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2019,3,15]]},"reference":[{"key":"40929_CR1","doi-asserted-by":"publisher","first-page":"54097","DOI":"10.1074\/jbc.M410234200","volume":"279","author":"Z Bercovich","year":"2004","unstructured":"Bercovich, Z. & Kahana, C. Degradation of antizyme inhibitor, an ornithine decarboxylase homologous protein, is ubiquitin-dependent and is inhibited by antizyme. J Biol Chem 279, 54097\u201354102, https:\/\/doi.org\/10.1074\/jbc.M410234200 (2004).","journal-title":"J Biol Chem"},{"key":"40929_CR2","doi-asserted-by":"publisher","first-page":"41504","DOI":"10.1074\/jbc.M407349200","volume":"279","author":"RM Newman","year":"2004","unstructured":"Newman, R. M. et al. Antizyme targets cyclin D1 for degradation. A novel mechanism for cell growth repression. J Biol Chem 279, 41504\u201341511, https:\/\/doi.org\/10.1074\/jbc.M407349200 (2004).","journal-title":"J Biol Chem"},{"key":"40929_CR3","doi-asserted-by":"publisher","DOI":"10.1186\/1471-2121-3-15","volume":"3","author":"Y Lin","year":"2002","unstructured":"Lin, Y. et al. A novel link between the proteasome pathway and the signal transduction pathway of the bone morphogenetic proteins (BMPs). BMC Cell Biol 3, 15 (2002).","journal-title":"BMC Cell Biol"},{"key":"40929_CR4","doi-asserted-by":"publisher","first-page":"6593","DOI":"10.1038\/sj.onc.1210482","volume":"26","author":"SK Lim","year":"2007","unstructured":"Lim, S. K. & Gopalan, G. Antizyme1 mediates AURKAIP1-dependent degradation of Aurora-A. Oncogene 26, 6593\u20136603, https:\/\/doi.org\/10.1038\/sj.onc.1210482 (2007).","journal-title":"Oncogene"},{"key":"40929_CR5","doi-asserted-by":"publisher","first-page":"1285","DOI":"10.1158\/1541-7786.MCR-11-0178","volume":"9","author":"RR Olsen","year":"2011","unstructured":"Olsen, R. R. & Zetter, B. R. Evidence of a role for antizyme and antizyme inhibitor as regulators of human cancer. Mol Cancer Res 9, 1285\u20131293, https:\/\/doi.org\/10.1158\/1541-7786.MCR-11-0178 (2011).","journal-title":"Mol Cancer Res"},{"key":"40929_CR6","doi-asserted-by":"crossref","unstructured":"Oredsson, S. M. Polyamine dependence of normal cell-cycle progression. Biochem Soc Trans 31, 366\u2013370, 10.1042\/ (2003).","DOI":"10.1042\/bst0310366"},{"key":"40929_CR7","doi-asserted-by":"publisher","first-page":"1090","DOI":"10.1093\/carcin\/bgi343","volume":"27","author":"DJ Feith","year":"2006","unstructured":"Feith, D. J., Origanti, S., Shoop, P. L., Sass-Kuhn, S. & Shantz, L. M. Tumor suppressor activity of ODC antizyme in MEK-driven skin tumorigenesis. Carcinogenesis 27, 1090\u20131098, https:\/\/doi.org\/10.1093\/carcin\/bgi343 (2006).","journal-title":"Carcinogenesis"},{"key":"40929_CR8","doi-asserted-by":"publisher","first-page":"3376","DOI":"10.1074\/jbc.272.6.3376","volume":"272","author":"D Yang","year":"1997","unstructured":"Yang, D. et al. Interleukin-1-induced growth inhibition of human melanoma cells. Interleukin-1-induced antizyme expression is responsible for ornithine decarboxylase activity down-regulation. 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