Broad-Spectrum Proteome Editing with an Engineered Bacterial Ubiquitin Ligase Mimic.

ABSTRACT: Manipulation of the ubiquitin-proteasome pathway to achieve targeted silencing of cellular proteins has emerged as a reliable and customizable strategy for remodeling the mammalian proteome. One such approach involves engineering bifunctional proteins called ubiquibodies that are comprised of a synthetic binding protein fused to an E3 ubiquitin ligase, thus enabling post-translational ubiquitination and degradation of a target protein independent of its function. Here, we have designed a panel of new ubiquibodies based on E3 ubiquitin ligase mimics from bacterial pathogens that are capable of effectively interfacing with the mammalian proteasomal degradation machinery for selective removal of proteins of interest. One of these, the Shigella flexneri effector protein IpaH9.8 fused to

SUBMITTER: Ludwicki MB 

PROVIDER: S-EPMC6535771 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature