NF-KAPPA-B P100 IS ONE OF THE HIGH-MOLECULAR-WEIGHT PROTEINS COMPLEXED WITH THE V-REL ONCOPROTEIN IN TRANSFORMED CHICKEN SPLEEN-CELLS

Authors
Citation
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
Citations number
46
Categorie Soggetti
Virology
Journal title
ISSN journal
0022538X
Volume
67
Issue
12
Year of publication
1993
Pages
7612 - 7617
Database
ISI
SICI code
0022-538X(1993)67:12<7612:NPIOOT>2.0.ZU;2-F
Abstract
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.