EFFECTS ON NF-KAPPA-B1 P105 PROCESSING OF THE INTERACTION BETWEEN THEHTLV-1 TRANSACTIVATOR TAX AND THE PROTEASOME/

THE viral Tax protein, which is encoded by human T-cell leukaemia viru s HTLV-I, activates nuclear translocation of the NF-kappa B/Rel transc ription factors and relieves cytoplasmic sequestration of RelA and Rel by heterodimerizatian with NF-kappa B1/p105 (refs 1,2). Proleolytic m aturation of this precursor protein is performed by the proteasome com plex(3,4). Here we show that Tax binds specifically to two subunits of the 20S proteasome, HsN3 and HC9. This Interaction is weakened with H sN3 and last for HC9 when a mutant of Tax is substituted that is selec tively defective for NF-kappa B activation. Immunoprecipitation shows that p105 binds weakly to HC9 and that this interaction is reinforced by Tax. No bridging function of Tax between p105 and HsN3 was observed . From these results, we propose that Tax accelerates the proteolytic maturation of p105 by favouring its anchorage to the proteasome.