Reduction/oxidation-phosphorylation control of DNA binding in the bZIP dimerization network

• Published in: BMC genomics 2006-05, Vol.7 (1), p.107-107, Article 107
• Main Authors: Amoutzias, Gregory D, Bornberg-Bauer, Erich, Oliver, Stephen G, Robertson, David L
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Dimerization; DNA - chemistry; DNA-Binding Proteins - chemistry; Humans; Molecular Sequence Data; Oxidation-Reduction; Oxidative Stress; Phosphorylation; Protein Binding; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Transcription Factors - chemistry
• ISSN: 1471-2164; 1471-2164
• DOI: 10.1186/1471-2164-7-107

bZIPs are transcription factors that are found throughout the eukarya from fungi to flowering plants and mammals. They contain highly conserved basic region (BR) and leucine zipper (LZ) domains and often function as environmental sensors. Specifically, bZIPs frequently have a role in mediating the response to oxidative stress, a crucial environmental signal that needs to be transduced to the gene regulatory network. Based on sequence comparisons and experimental data on a number of important bZIP transcription factors, we predict which bZIPs are under redox control and which are regulated via protein phosphorylation. By integrating genomic, phylogenetic and functional data from the literature, we then propose a link between oxidative stress and the choice of interaction partners for the bZIP proteins. This integration permits the bZIP dimerization network to be interpreted in functional terms, especially in the context of the role of bZIP proteins in the response to environmental stress. This analysis demonstrates the importance of abiotic factors in shaping regulatory networks.