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Dechend, R.* ; Hirano, F.* ; Lehmann, K.* ; Heissmeyer, V.* ; Ansieau, S.* ; Wulczyn, F.G.* ; Scheidereit, C.* ; Leutz, A.*

The Bcl-3 oncoprotein acts as a bridging factor between NF-kappa B/Rel and nuclear co-regulators.

Oncogene 18, 3316-3323 (1999)
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Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
The proto-oncoprotein Bcl-3 is a member of the I kappa B family and is present predominantly in the nucleus. To gain insight into specific nuclear functions of Bcl-3 we have isolated proteins that interact with its ankyrin repeat domain. Using the yeast two-hybrid-system we identified four novel binding partners of Bcl-3 in addition to NF-kappa B p50 and p52, previously known to associate with Bcl-3. The novel Bcl-3 interactors Jab1, Pirin, Tip60 and Bard1 are nuclear proteins which also bind to other transcription factors including c-Jun, nuclear factor I (NFI), HIV-1 Tat or the tumor suppressor and Polll holoenzyme component Brca1, respectively. Bcl-3, p50, and either Bard1, Tip60 or Pirin are sequestered into quarternary complexes on NF-kappa B DSA binding sites, whereas Jab1 enhances p50-Bcl-3-DNA complex formation. Furthermore, the histone acetylase Tip60 enhances Bcl-3-p50 activated transcription through an NF-kappa B binding site, indicating that quarternary complexes containing Bcl-3 interactors modulate NF-kappa B driven gene expression, These data implicate Bcl-3 as an adaptor between NF-kappa B p50/p52 and other transcription regulators and suggest that its gene activation function may at least in part be due to recruitment of the Tip60 histone actetylase.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Oncogene ; Coactivator ; Chromatin ; Gene Regulation ; Signal Transduction; Candidate Protooncogene Bcl-3; Dna-binding; B Proteins; Transcriptional Activation; P50 Homodimers; Human Genes; In-vivo; Brca1; Encodes; Phosphorylation
ISSN (print) / ISBN 0950-9232
e-ISSN 0950-9232
Zeitschrift Oncogene
Quellenangaben Band: 18, Heft: 22, Seiten: 3316-3323 Artikelnummer: , Supplement: ,
Verlag Nature Publishing Group
Verlagsort Basingstoke
Begutachtungsstatus Peer reviewed