The HBP-1 family of wheat basic/leucine zipper proteins interacts with overlapping cis-acting hexamer motifs of plant histone genes.

The type I element (CCACGTCANCGATCCGCG) is a cis-acting element that is essential for the transcriptional regulation of the wheat histone H3 (TH012) gene. The sequence CCACGTCA in the type I element resembles various plant regulatory elements that share an ACGT core sequence, which can be recognized by different basic/leucine zipper (bZIP) proteins. Here we describe the isolation and characterization of wheat cDNA clones encoding three novel bZIP proteins, designated HBP (histone promoter-binding protein)-1a(1), HBP-1a(c14), and HBP-1b(c1). These proteins specifically bind to the ACGT core sequence and, together with previously identified HBP-1a(17) and HBP-1b(c38), constitute a protein family, named the HBP-1 family. Based on their structural characteristics and DNA binding specificities, members of the HBP-1 family can be grouped into HBP-1a and HBP-1b subfamilies. The HBP-1a isoforms are characterized by their N-terminal proline-rich domain and a C-terminal bZIP domain, which binds to the CCACGT motif. In contrast, the HBP-1b isoforms have a bZIP domain at the N terminus, which binds to the ACGTCA motif, and a glutamine-rich domain at the C terminus. All members of both subfamilies interact with the CCACGTCA sequence, but their DNA binding specificities and affinities differ. Since HBP-1a isoforms form heterodimers in all pairwise combinations, heterodimer formation among these bZIP proteins may generate an expanded repertoire of regulatory potential for gene expression in plants.