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J Biol Chem, Vol. 273, Issue 6, 3180-3191, February 6, 1998

Amino Acid Analogs Activate NF-B through Redox-dependent IB- Degradation by the Proteasome without Apparent IB- Phosphorylation
CONSEQUENCE ON HIV-1 LONG TERMINAL REPEAT ACTIVATION

From the Laboratoire du Stress Cellulaire, Centre de Génétique Moléculaire et Cellulaire, CNRS-UMR 5534, Université Claude Bernard Lyon-I, 69622 Villeurbanne Cedex, France

We report here that amino acid analogs, which activate hsp70 promoter, are powerful transcriptional activators of human immunodeficiency virus 1 (HIV-1) long terminal repeat (LTR), an activation which was impaired when the two B sites present in the LTR were mutated or deleted. Amino acid analogs also stimulated the transcription of a B-controlled reporter gene. Upon treatment with amino acid analogs, the two NF-B subunits (p65 and p50), which are characterized by a relatively long half-life, redistributed into the nucleus where they bound to B elements. This phenomenon, which began to be detectable after 1 h of treatment, was concomitant with the degradation of the short lived inhibitory subunit IB- by the proteasome. However, contrasting with other NF-B inducers that trigger IB- degradation through a phosphorylation step, amino acid analogs did not change IB- isoform composition. Antioxidant conditions inhibited amino acid analog stimulatory action toward NF-B. This suggests that aberrant protein conformation probably generates a pro-oxidant state that is necessary for IB- proteolysis by the proteasome. Moreover, this activation of NF-B appeared different from that mediated by endoplasmic reticulum overload as it was not inhibited by calcium chelation.

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