CREB/ATF BZIP Transcription Factor (CREBZF)

Sequence analysis predicted that the 272-amino acid ZF protein has a negatively charged N terminus, a basic domain and a leucine zipper of 6 heptad leucine repeats separated by a conserved 6-amino acid spacer, and a bZIP region. Functional analysis showed that the N-terminal acidic region is an activation domain. EMSA analysis indicated, however, that ZF could not activate bZIP-type promoters, possibly due to an N-terminal conformational change resulting from the lack of a critical asn residue. Functional and binding analyses indicated that ZF interacted with HCFC1 without interfering with VP16 binding, whereas 3 ZF mutants did not interact with HCFC1. In addition, most cells expressing ZF appeared to be nonpermissive for HSV infection.