High-mobility group protein A1 binds herpes simplex virus gene regulatory sequences and affects their expression.

The high-mobility group protein A1 (HMGA1), which regulates mammalian gene expression by altering chromatin architecture, was found to bind at multiple sites within the promoter regions of all of the herpes simplex virus type 1 (HSV-1) immediate early genes, as well as a representative early (tk) gene and one late (gC) gene, both in vitro and in vivo. Infected cell polypeptide (ICP) 4, the major HSV-1 regulatory protein, binds these promoters both in vitro and in vivo, and HMGA1 enhances its in vitro binding. In transient expression experiments, HMGA1 modified the effects of both ICP4 and ICP0, another virus transactivator, on virus gene expression in a promoter-specific manner, but it had no effect on the transactivation of immediate-early promoters by VP16.

Interactions of the antizyme AtoC with regulatory elements of the Escherichia coli atoDAEB operon.

AtoC has a dual function as both an antizyme, the posttranslational inhibitor of polyamine biosynthetic enzymes, and the transcriptional regulator of genes involved in short-chain fatty acid catabolism (the atoDAEB operon). We have previously shown that AtoC is the response regulator of the AtoS-AtoC two-component signal transduction system that activates atoDAEB when Escherichia coli is exposed to acetoacetate. Here, we show that the same cis elements control both promoter inducibility and AtoC binding.