Networks of bZIP Protein-Protein Interactions Diversified Over a Billion Years of Evolution

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Science  10 May 2013:
Vol. 340, Issue 6133, pp. 730-734
DOI: 10.1126/science.1233465

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bZIPping Through Evolution

The basic region-leucine zipper (bZIP) transcription factors are found in many species and can form complexes that bind to DNA and affect transcription. Reinke et al. (p. 730) analyzed interactions for over 3000 bZIPs within and among five metazoan and two unicellular species. The results reveal differences within bZIP interactive networks that have accumulated over time and identify plasticity among interactions and changes in binding specificity that relate to specific amino acid residue changes.


Differences in biomolecular sequence and function underlie dramatic ranges of appearance and behavior among species. We studied the basic region-leucine zipper (bZIP) transcription factors and quantified bZIP dimerization networks for five metazoan and two single-cell species, measuring interactions in vitro for 2891 protein pairs. Metazoans have a higher proportion of heteromeric bZIP interactions and more network complexity than the single-cell species. The metazoan bZIP interactomes have broadly similar structures, but there has been extensive rewiring of connections compared to the last common ancestor, and each species network is highly distinct. Many metazoan bZIP orthologs and paralogs have strikingly different interaction specificities, and some differences arise from minor sequence changes. Our data show that a shifting landscape of biochemical functions related to signaling and gene expression contributes to species diversity.

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