Ghosh S, Gifford A M, Riviere L R, Tempst P, Nolan G P, Baltimore D
Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, Massachusetts 02142.
Cell. 1990 Sep 7;62(5):1019-29. doi: 10.1016/0092-8674(90)90276-k.
The DNA binding subunit of the transcription factor NF-kappa B, p50, has been cloned. p50 appears to be synthesized as a larger protein that is then processed to its functional size. Sequence analysis reveals remarkable homology for over 300 amino acids at the amino-terminal end to the oncogene v-rel, its cellular homolog c-rel, and the Drosophila maternal effect gene dorsal. This establishes NF-kappa B as a member of the rel family of proteins, all of which display nuclear-cytosolic translocation. Protein sequence from the p65 polypeptide has established that it is not encoded in the same mRNA as p50. However, p65 appears homologous to c-rel, suggesting that c-rel may form heterodimers with p50 and rel may include a homodimerization motif.
