Ora Schueler-Furman

Abstract The ubiquitin-specific proteases (USPs) family is the largest family of human deubiquitinating enzymes (DUBs). While most USPs are agnostic to polyubiquitin linkage-type, their substrate specificity is thought to be mediated by the recognition of the ubiquitnated protein itself. In addition to their catalytic domain, USPs have one or more auxiliary domains (ADs) with key functions in regulating DUB activity and localization.

Keywords bacterial cell poles high-throughput screens 3D interaction modeling protein-protein interaction subcellular localization in bacteria PTS enzyme I, EI TmaR phase separation, PS Research topic(s) CP: Microbiology CP: Molecular biology Introduction The complexity of bacterial cells has been underestimated for decades. The scarcity of membrane-bounded organelles led to the assumption that macromolecules are not specifically localized in bacterial cells.

Graphical Abstract Chang and Perez suggest a simple and elegant approach for using AlphaFold2 to determine relative binding preferences of a receptor for two of its peptide substrates: when presented with both peptides, AlphaFold2 models only the stronger binder into the binding site. This easy approach will help many biologists to quickly estimate best binders and accelerate research on peptide substrate-mediated interactions.