In Science this week, researchers from McGill University reported new details about the activation of Parkin, a gene that, when mutated, is responsible for an autosomal recessive form of Parkinson’s disease. Using x-ray scattering, the team determined the crystal structure of the full-length parkin protein in rat tissue. The protein is ordinarily inactive, but they found that mutations that the disrupted two inhibitory binding interactions activated it. The findings may offer insights into enhancing parkin’s neuroprotective activity.
Also in Science, investigators from the Massachusetts Institute of Technology published new data detailing how changes in certain protein-protein have contributed to species diversity. The scientists examined the basic region-leucine zipper, or bZIP, transcription factors and quantified bZIP dimerization networks for five metazoan and two single-cell species, measuring interactions in vitro for 2,891 protein pairs.
They found that metazoan bZIP interactomes have “broadly similar structures,” yet there has been “extensive rewiring of connections compared to the last common ancestor.” At the same time, each species network is highly distinct, and many metazoan bZIP orthologs and paralogs display “strikingly different” interaction specificities.”
Overall, the data suggest that the changes in biochemical functions related to signaling and gene expression had a major impact on the rise of different species.