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Spodoptera frugiperda FKBP‐46 is a consensus p53 motif binding protein
Author(s) -
Mohareer Krishnaveni,
Sahdev Sudhir,
Hasnain Seyed E.
Publication year - 2013
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.24429
Subject(s) - fkbp , biology , spodoptera , binding protein , schneider 2 cells , drosophila melanogaster , sequence motif , conserved sequence , microbiology and biotechnology , dna , peptide sequence , biochemistry , rna interference , gene , recombinant dna , rna
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 ( Sf 9) insect cells, which is activated during oxidative stress, caused by exposure to UV‐B or H 2 O 2 , and binds to p53 consensus DNA binding motifs as well as other p53 cognate motifs. Sf 9 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 Sf 9 p53 motif‐binding protein reveals extensive homology to the pro‐apoptotic FK‐506 binding protein (FKBP‐46), earlier identified in Sf 9 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.

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