Spodoptera frugiperda FKBP-46 is a consensus p53 motif binding protein
Article first published online: 18 FEB 2013
Copyright © 2012 Wiley Periodicals, Inc.
Journal of Cellular Biochemistry
Volume 114, Issue 4, pages 899–907, April 2013
How to Cite
Mohareer, K., Sahdev, S. and Hasnain, S. E. (2013), Spodoptera frugiperda FKBP-46 is a consensus p53 motif binding protein. J. Cell. Biochem., 114: 899–907. doi: 10.1002/jcb.24429
- Issue published online: 18 FEB 2013
- Article first published online: 18 FEB 2013
- Accepted manuscript online: 23 OCT 2012 11:58AM EST
- Manuscript Accepted: 15 OCT 2012
- Manuscript Received: 12 JUL 2011
- Spodoptera frugiperda;
- OXIDATIVE STRESS;
- Sf9 p53-LIKE FACTOR;
p53 protein, the central molecule of the apoptosis pathway, is mutated in 50% of the human cancers. Of late, p53 homologues have been identified from different invertebrates including Drosophila melanogaster, Caenorhabditis elegans, Squid, and Clams. We report the identification of a p53-like protein in Spodoptera frugiperda (Sf9) insect cells, which is activated during oxidative stress, caused by exposure to UV-B or H2O2, and binds to p53 consensus DNA binding motifs as well as other p53 cognate motifs. Sf9 p53 motif-binding protein is similar to murine and Drosophila p53 in terms of molecular size, which is around 50–60 kDa, as evident from UV cross-linking, and displays DNA binding characteristics similar to both insect and vertebrate p53 as seen from electrophoretic mobility shift assays. The N-terminal sequencing of the purified Sf9 p53 motif-binding protein reveals extensive homology to the pro-apoptotic FK-506 binding protein (FKBP-46), earlier identified in Sf9 cells as a factor which interacts with murine casein kinase. FKBP, an evolutionarily conserved protein of mammalian origin functions as a pro-apoptotic factor. Identification of FKBP-46 as a novel p53 motif-binding protein in insect cells adds a new facet to our understanding of the mechanisms of apoptosis under oxidative stress in the absence of a typical p53 homologue. J. Cell. Biochem. 114: 899–907, 2013. © 2012 Wiley Periodicals, Inc.