M MUROI, Y MUROI, K YAMAMOTO, T SUZUKI
JOURNAL OF BIOLOGICAL CHEMISTRY, 268(26) 19534-19539, Sep, 1993 Peer-reviewed
Lipopolysaccharide treatment of mouse macrophage-like J774 cells was found to result in the activation of three different nuclear proteins which specifically bind to oligonucleotide containing the NF-kappaB motif of the human immunodeficiency virus (HIV) gene. These are designated as NF-kappaB1, -kappaB2, and -kappaB3, according to their electrophoretic mobilities (fast, intermediate, and slow, respectively). Immunological and UV cross-linking studies showed that NF-kappaB1 consists of only p50 subunit, whereas both NF-kappaB2 and -kappaB3 contain NF-kappaB p65 subunit and c-Rel. In addition, NF-kappaB2 was also found to contain p50 subunit of NF-kappaB. The binding of three types of NF-kappaB proteins to HIV NF-kappaB motif was effectively inhibited by other NF-kappaB motifs, whose 3' half-site nucleotide sequences are T/A-T-T/C-CC (HIV, interleukin-6, interferon (INF)-beta, H2-K(b), I-Ealpha(d), and TNF-alpha2 (nucleotide position -510)) and much less effectively by NF-kappaB motifs with 3' half-site sequences of TGCCC (TNF-alpha3, nucleotide position -610), ATCTC (G-CSF), TATTC (FcgammaR), or TCCTT (TNF-alpha1, nucleotide position -850). Our data also suggested that NF-kappaB1 and -kappaB2 which contain p50 subunit of NF-kappaB bind with the higher preference for NF-kappaB motif of H2-K(b) gene promoter than that of INF-beta, whereas NF-kappaB3 which does not contain p50 subunit appears to preferentially bind to NF-kappaB sites of IFN-beta.