Effects on NF-kappa B1/p105 processing of the interaction between the HTLV-1 transactivator Tax and the proteasome.
The viral Tax protein, which is encoded by human T-cell leukaemia virus HTLV-I, activates nuclear translocation of the NF-kappa B/Rel transcription factors and relieves cytoplasmic sequestration of RelA and Rel by heterodimerization with NF-kappa B1/p1O5 (refs 1,2). Proteolytic maturation of this precursor protein is performed by the proteasome complex. Here ... we show that Tax binds specifically to two subunits of the 20S proteasome, HsN3 and HC9. This interaction is weakened with HsN3 and lost for HC9 when a mutant of Tax is substituted that is selectively defective for NF-kappa B activation. Immunoprecipitation shows that p1O5 binds weakly to HC9 and that this interaction is reinforced by Tax. No bridging function of Tax between p1O5 and HsN3 was observed. From these results, we propose that Tax accelerates the proteolytic maturation of P105 by favouring its anchorage to the proteasome.
Mesh Terms:
Cell Line, Cloning, Molecular, Cysteine Endopeptidases, Gene Products, tax, Human T-lymphotropic virus 1, Humans, Multienzyme Complexes, NF-kappa B, NF-kappa B p50 Subunit, Point Mutation, Proteasome Endopeptidase Complex, Protein Binding, Protein Precursors, Protein Processing, Post-Translational, Saccharomyces cerevisiae, Transfection
Cell Line, Cloning, Molecular, Cysteine Endopeptidases, Gene Products, tax, Human T-lymphotropic virus 1, Humans, Multienzyme Complexes, NF-kappa B, NF-kappa B p50 Subunit, Point Mutation, Proteasome Endopeptidase Complex, Protein Binding, Protein Precursors, Protein Processing, Post-Translational, Saccharomyces cerevisiae, Transfection
Nature
Date: May. 23, 1996
PubMed ID: 8692272
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