NF-kappaB precursor p100 inhibits nuclear translocation and DNA binding of NF-kappaB/rel-factors

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Item Type:	Article
Title:	NF-kappaB precursor p100 inhibits nuclear translocation and DNA binding of NF-kappaB/rel-factors
Creators Name:	Naumann, M., Nieters, A., Hatada, E.N. and Scheidereit, C.
Abstract:	The NF-kappa B precursor p100 (lyt-10, p97, p98) generates after proteolytic processing a 52 kDa subunit, which can bind to kappa B-motifs. A deregulated form of the p100 gene, which is structurally altered by a t(10;14) translocation, has a potential oncogenic role in certain human B cell lymphomas. In this study p100 was analysed for its ability to interact with its own processing product p52, with p50, the product of the NF-kappa B precursor p105, and with other NF-kappa B/rel-proteins. As demonstrated by a combination of Western blot analysis, band shift analysis and indirect immunofluorescence labelling of transfected cells, p100 itself was localized in the cytoplasm and indiscriminately retained each co-expressed NF-kappa B subunit. Thereby it simultaneously inhibited their DNA binding activities. Thus, a major function of p100 is, like p105, to associate with subunits of the rel multigene family in the cytoplasm in an I kappa B-like fashion. The similarity between p100 and p105 is also reflected by equivalent protein interactions of their processing products: like NF-kappa B-p50, also NF-kappa B-p52 heteromerised promiscuously with all rel-factors tested. Moreover, p52 efficiently interacts with the candidate oncogene product Bcl-3 and also binds to the basic-leucine zipper protein NF-IL6.
Keywords:	Amino Acid Sequence, Biological Transport, Cell Line, Cell Nucleus, DNA, Molecular Sequence Data, NF-kappa B, NF-kappa B p50 Subunit, Protein Precursors, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-rel, Animals
Source:	Oncogene
ISSN:	0950-9232
Publisher:	Nature Publishing Group
Volume:	8
Number:	8
Page Range:	2275-2281
Date:	1 August 1993
PubMed:	View item in PubMed

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