| Abstract: |
The Rel-associated protein pp40 is functionally related to IκB, an inhibitor of the transcription factor NF-κB. Purified pp40 inhibits the DNA binding activity of the NF-κB protein complex (p50:p65 heterodimers), p50:c-Rel heteromers, and c-Rel homodimers. The sequence of the complementary DNA encoding pp40 revealed similarity to the gene encoding MAD-3, a protein with mammalian IκB-like activity. Protein sequencing of IκB purified from rabbit lung confirmed that MAD-3 encodes a protein similar to IκB. The sequence similarity between MAD-3 and pp40 includes a casein kinase II and consensus tyrosine phosphorylation site, as well as five repeats of a sequence found in the human erythrocyte protein ankyrin. These results suggest that rel-related transcription factors, which are capable of cytosolic to nuclear translocation, may be held in the cytosol by interaction with related cytoplasmic anchor molecules. |
| Keywords: |
nonhuman; comparative study; animal; mammalia; animal tissue; cells, cultured; proto oncogene; transcription factor; animalia; transcription factors; cloning, molecular; amino acid sequence; molecular sequence data; rna, messenger; nf-kappa b; lung; phosphoproteins; base sequence; dna sequence; sequence homology, nucleic acid; complementary dna; chick embryo; open reading frames; inhibitor protein; rabbit; dna probes; oncogene proteins v-rel; oryctolagus cuniculus; protein-tyrosine kinase; oligonucleotide probes; priority journal; article; staphylococcus phage 3a; support, non-u.s. gov't; support, u.s. gov't, p.h.s.; retroviridae proteins, oncogenic
|
