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J Biol Chem, Vol. 275, Issue 7, 4719-4725, February 18, 2000
From the Department of Biochemistry, Division of Gene Expression
and Regulation, MSI/WTB Complex, Dow Street, University of Dundee,
Dundee, DD1 5EH Scotland, United Kingdom
Induction of transcription from the human
immunodeficiency virus 1 long terminal repeat by the RelA (p65) NF-
Inhibition of the RelA(p65) NF-
B Subunit by Egr-1*
and
B
subunit has been shown to be dependent upon an interaction with the
zinc finger DNA-binding domain of Sp1. It was unknown, however, whether
NF-B could also interact with other zinc finger-containing
transcription factors. In this study we demonstrate that the early
growth response transcription factor Egr-1, whose DNA-binding domain
shares a high degree of homology with that of Sp1, can also interact
with RelA in vitro and regulate NF-B transcriptional
activity in vivo. Similar to the interaction with Sp1, the
Rel homology domain of RelA interacts with the zinc finger domain of
Egr-1. Surprisingly, and in contrast to Sp1, Egr-1 specifically
represses RelA transcriptional activity through its zinc finger domain.
Moreover, the interaction between RelA and the Egr-1 zinc fingers is
mutually exclusive with DNA binding suggesting a model in which Egr-1
directly sequesters NF-B from its target promoters. Because Egr-1 is
induced by many of the same stimuli that activate NF-B, this novel
transcriptional regulatory mechanism has many implications for the
involvement of both factors in cellular processes such as apoptosis and
the response to stress and infection.
*
This work was supported in part by Tenovus.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported by a grant from the Medical Research Council.
§
Supported by a Royal Society University Fellowship. To whom
correspondence should be addressed. Tel.: 44 1382 345 606; Fax: 44 1382 348 072; E-mail: nperkins@bad.dundee.ac.uk.
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