Open AccessThe NF-kappa B-binding site mediates phorbol ester-inducible transcription in nonlymphoid cells.
Author(s) -
Barbara Nelsen,
Lars Hellman,
Ranjan Sen
Publication year - 1988
Publication title -
molecular and cellular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.14
H-Index - 327
eISSN - 1067-8824
pISSN - 0270-7306
DOI - 10.1128/mcb.8.8.3526
Subject(s) - enhancer , biology , transcription factor , microbiology and biotechnology , transcription (linguistics) , nfkb1 , dna binding protein , nuclear protein , dna , phorbol , tetradecanoylphorbol acetate , binding site , gene , biochemistry , signal transduction , protein kinase c , linguistics , philosophy
The mouse immunoglobulin kappa light-chain enhancer can interact with at least three independent nuclear proteins. One of these proteins, NF-kappa B, is constitutively present only in nuclear extracts derived from B cells and plasma cells. A DNA-binding protein with the same sequence specificity (and therefore presumed to be NF-kappa B itself) can be induced in pre-B cells, T cells, and nonlymphoid cells by phorbol 12-acetate-13-myristate (PMA); however, it is not clear whether the induced factor can activate transcription in nonlymphoid cells as NF-kappa B does in B cells. In this paper we show that multimerization of a fragment of the mouse kappa enhancer that carried only the binding site for NF-kappa B behaved like a B-cell-specific regulatory element. Furthermore, this unit served to activate transcription in nonlymphoid cells after treatment with PMA (but not with cyclic AMP derivatives), and the kinetics of transcription activation correlated well with the kinetics of factor induction. Thus, the induced DNA-binding activity appeared to be functionally indistinguishable from that of NF-kappa B.