c-rel activates but v-rel suppresses transcription from kappa B sites.

AUTOR(ES)

Inoue, J

RESUMO

We show that the product of the protooncogene c-rel is a constituent of an NF-kappa B-like complex that binds to the kappa B site originally identified in the enhancer of immunoglobulin kappa light chain gene. c-rel protein synthesized in bacteria binds to the kappa B site in a sequence-specific manner. The rel-kappa B complex can be disrupted by incubation with anti-rel antibodies. The rel protein can form oligomers. The c-rel protein can activate transcription from promoters containing kappa B sites; v-rel, on the other hand, suppresses the transcription of genes linked to kappa B sites. Thus, v-rel may interfere with the normal transcriptional machinery of the cell by acting as a dominant negative mutant.

Documentos Relacionados

• Avian I kappa B alpha is transcriptionally induced by c-Rel and v-Rel with different kinetics.
• PEST-dependent cytoplasmic retention of v-Rel by I(kappa)B-alpha: evidence that I(kappa)B-alpha regulates cellular localization of c-Rel and v-Rel by distinct mechanisms.
• Functional interaction of the v-Rel and c-Rel oncoproteins with the TATA-binding protein and association with transcription factor IIB.
• Differential Regulation of the Inhibitor of Apoptosis ch-IAP1 by v-rel and the Proto-Oncogene c-rel
• v-rel induces expression of three avian immunoregulatory surface receptors more efficiently than c-rel.