S. Sif et Td. Gilmore, NF-KAPPA-B P100 IS ONE OF THE HIGH-MOLECULAR-WEIGHT PROTEINS COMPLEXED WITH THE V-REL ONCOPROTEIN IN TRANSFORMED CHICKEN SPLEEN-CELLS, Journal of virology, 67(12), 1993, pp. 7612-7617
The Rel/NF-kappaB family of proteins includes several interacting cell
ular transcription factors and the v-Rel oncoprotein of the avian Rev-
T retrovirus. We report the isolation of a chicken cDNA for the NF-kap
paB p52 precursor protein p100. Full-length p100 only weakly binds DNA
in vitro; removal of the ankyrin-like repeats generates C-terminally
truncated p100 proteins (like p52) that have an increased ability to b
ind an oligonucleotide containing a kappaB site. In addition, we show
that chicken p100 is identical to a protein previously designated p115
, which is found in a complex with v-Rel in transformed chicken spleen
cells. Furthermore, p100 and v-Rel can form a complex when synthesize
d in vitro. Using cDNAs for chicken NF-kappaB p105, NF-kappaB p100, c-
Rel, and v-Rel, we show that one of the complexes in v-Rel-transformed
spleen cells can be reconstituted in vitro.