The C6 zinc cluster dictates asymmetric binding by HAP1.
AUTOR(ES)
Zhang, L
RESUMO
Unlike other C6 zinc cluster proteins such as GAL4 and PPR1, HAP1 binds selectively to asymmetric DNA sites containing a direct repeat of two CGG triplets. Here, we show that the HAP1 zinc cluster is solely responsible for asymmetric binding by HAP1. An asymmetric interaction between two zinc clusters of a HAP1 dimer must position the zinc clusters in a directly repeated orientation, and enable them to recognize two CGG triplets in a direct repeat. Further, our data suggest that this asymmetric interaction acts cooperatively with the interaction between dimerization elements to promote HAP1 dimerization, and locks HAP1-DNA complexes in a stable, dimeric conformation.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=452199Documentos Relacionados
- Comparative amino acid sequence analysis of the C6 zinc cluster family of transcriptional regulators.
- Antibody-promoted dimerization bypasses the regulation of DNA binding by the heme domain of the yeast transcriptional activator HAP1.
- Yeast SNF1 protein kinase interacts with SIP4, a C6 zinc cluster transcriptional activator: a new role for SNF1 in the glucose response.
- An n-Alkane-Responsive Promoter Element Found in the Gene Encoding the Peroxisomal Protein of Candida tropicalis Does Not Contain a C6 Zinc Cluster DNA-Binding Motif
- Asparagine 212 is essential for abasic site recognition by the human DNA repair endonuclease HAP1.