Precise details of how a master regulator of gene expression binds its activating partner could open new avenues for cancer drug development.

The findings reveal how the activating partner, a small cellular metabolite and signaling molecule called PI5P, interacts simultaneously with two different regions of the regulatory protein UHRF1. This shows how, when it comes to the modulation of complex proteins, binding arrangements can take on elaborate multipart forms.

The interaction between PI5P and UHRF1 thus exemplifies the old adage "The whole is greater than the sum of its parts." As Wolfgang Fischle, KAUST biochemist and study author, points out: “Regions linking separate domains of a multidomain protein can have important functionality in organizing and thereby regulating the overall structure and function of a protein.”

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Image: KAUST researchers are revealing new details about the protein UHRF1, which is one of the most potent targets for cancer therapeutics.
© 2022 KAUST; Anastasia Serin.