An interaction between the DNA-binding domains of RelA(p65) and Sp1 mediates human immunodeficiency virus gene activation.

摘要: Induction of human immunodeficiency virus type 1 (HIV-1) gene expression in stimulated T cells has been attributed to the activation transcription factor NF-kappa B. The twice-repeated kappa B sites within HIV-1 long terminal repeat are close proximity three binding for Sp1. We have previously shown that a cooperative interaction with Sp1 is required efficient stimulation transcription. In this report, we define domains each protein responsible effect. Although transactivation seemed likely mediate interaction, find, surprisingly, occurs through putative DNA-binding both proteins. specifically interacted amino-terminal region RelA(p65). Similarly, RelA bound directly zinc finger This was specific and resulted DNA repeat. Furthermore, did not associate several other factors, including MyoD, E12, or Kox15, another protein. These findings suggest juxtaposition promotes between regions these factors. HIV transcriptional may provide mechanism allow selective B-regulated genes.