Toxin-based screening of C-terminal tags in Escherichia coli reveals the exceptional potency of ssrA-like degrons.

ABSTRACT: All bacteria possess ATP-dependent proteases that destroy cytosolic proteins. These enzymes help cells mitigate proteotoxic stress, adapt to changing nutrient availability, regulate virulence phenotypes, and transition to pathogenic lifestyles. Moreover, ATP-dependent proteases have emerged as promising antibacterial and antivirulence targets in a variety of pathogens. The physiological roles of these proteases are largely defined by the complement of proteins that they degrade. Substrates are typically recognized in a highly selective manner, often via short unstructured sequences termed degrons. While a few degrons have been identified and rigorously characterized, we lack a systematic understanding of how proteases select valid degrons from the vast complexity of protein sequence space.

SUBMITTER: Beardslee PC 

PROVIDER: S-EPMC10862746 | biostudies-literature | 2024 Apr

REPOSITORIES: biostudies-literature