Abstract
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-κB motif of the human immunodeficiency virus (HIV) gene. These are designated as NF-κB1, -κB2, and -κB3, according to their electrophoretic mobilities (fast, intermediate, and slow, respectively). Immunological and UV cross-linking studies showed that NF-κB1 consists of only p50 subunit, whereas both NF-κB2 and -κB3 contain NF-κB p65 subunit and c-Rel. In addition, NF-κB2 was also found to contain p50 subunit of NF-κB. The binding of three types of NF-κB proteins to HIV NF-κB motif was effectively inhibited by other NF-κB motifs, whose 3′ half-site nucleotide sequences are T/A-T-T/C-CC (HIV, interleukin-6, interferon (INF)-β, H2-Kb, I-Eαd, and TNF-α2 (nucleotide position -510)) and much less effectively by NF-κB motifs with 3′ half-site sequences of TGCCC (TNF-α3, nucleotide position -610), ATCTC (G-CSF), TATTC (FcγR), or TCCTT (TNF-α1, nucleotide position -850). Our data also suggested that NF-κB1 and -κB2 which contain p50 subunit of NF-κB bind with the higher preference for NF-κB motif of H2-Kb gene promoter than that of INF-β, whereas NF-κB3 which does not contain p50 subunit appears to preferentially bind to NF-κB sites of IFN-β.
| Original language | English |
|---|---|
| Pages (from-to) | 19534-19539 |
| Number of pages | 6 |
| Journal | Journal of Biological Chemistry |
| Volume | 268 |
| Issue number | 26 |
| Publication status | Published - Sep 15 1993 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
Cite this
Influence of 3′ half-site sequence of NF-κB motifs on the binding of lipopolysaccharide-activatable macrophage NF-κB proteins. / Muroi, Masashi; Muroi, Yukiko; Yamamoto, Ken-ichi; Suzuki, Tsuneo.
In: Journal of Biological Chemistry, Vol. 268, No. 26, 15.09.1993, p. 19534-19539.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Influence of 3′ half-site sequence of NF-κB motifs on the binding of lipopolysaccharide-activatable macrophage NF-κB proteins
AU - Muroi, Masashi
AU - Muroi, Yukiko
AU - Yamamoto, Ken-ichi
AU - Suzuki, Tsuneo
PY - 1993/9/15
Y1 - 1993/9/15
N2 - 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-κB motif of the human immunodeficiency virus (HIV) gene. These are designated as NF-κB1, -κB2, and -κB3, according to their electrophoretic mobilities (fast, intermediate, and slow, respectively). Immunological and UV cross-linking studies showed that NF-κB1 consists of only p50 subunit, whereas both NF-κB2 and -κB3 contain NF-κB p65 subunit and c-Rel. In addition, NF-κB2 was also found to contain p50 subunit of NF-κB. The binding of three types of NF-κB proteins to HIV NF-κB motif was effectively inhibited by other NF-κB motifs, whose 3′ half-site nucleotide sequences are T/A-T-T/C-CC (HIV, interleukin-6, interferon (INF)-β, H2-Kb, I-Eαd, and TNF-α2 (nucleotide position -510)) and much less effectively by NF-κB motifs with 3′ half-site sequences of TGCCC (TNF-α3, nucleotide position -610), ATCTC (G-CSF), TATTC (FcγR), or TCCTT (TNF-α1, nucleotide position -850). Our data also suggested that NF-κB1 and -κB2 which contain p50 subunit of NF-κB bind with the higher preference for NF-κB motif of H2-Kb gene promoter than that of INF-β, whereas NF-κB3 which does not contain p50 subunit appears to preferentially bind to NF-κB sites of IFN-β.
AB - 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-κB motif of the human immunodeficiency virus (HIV) gene. These are designated as NF-κB1, -κB2, and -κB3, according to their electrophoretic mobilities (fast, intermediate, and slow, respectively). Immunological and UV cross-linking studies showed that NF-κB1 consists of only p50 subunit, whereas both NF-κB2 and -κB3 contain NF-κB p65 subunit and c-Rel. In addition, NF-κB2 was also found to contain p50 subunit of NF-κB. The binding of three types of NF-κB proteins to HIV NF-κB motif was effectively inhibited by other NF-κB motifs, whose 3′ half-site nucleotide sequences are T/A-T-T/C-CC (HIV, interleukin-6, interferon (INF)-β, H2-Kb, I-Eαd, and TNF-α2 (nucleotide position -510)) and much less effectively by NF-κB motifs with 3′ half-site sequences of TGCCC (TNF-α3, nucleotide position -610), ATCTC (G-CSF), TATTC (FcγR), or TCCTT (TNF-α1, nucleotide position -850). Our data also suggested that NF-κB1 and -κB2 which contain p50 subunit of NF-κB bind with the higher preference for NF-κB motif of H2-Kb gene promoter than that of INF-β, whereas NF-κB3 which does not contain p50 subunit appears to preferentially bind to NF-κB sites of IFN-β.
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UR - http://www.scopus.com/inward/citedby.url?scp=0027268399&partnerID=8YFLogxK
M3 - Article
VL - 268
SP - 19534
EP - 19539
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 26
ER -