TY - DATA T1 - Dataset for: The regulatory significance of tag recycling in the mycobacterial Pup-proteasome system PY - 2017/05/12 AU - Yifat Elharar AU - Shai Schlussel AU - Nir Hecht AU - Michael M. Meijler AU - Eyal Gur UR - https://wiley.figshare.com/articles/dataset/Dataset_for_The_regulatory_significance_of_tag_recycling_in_the_mycobacterial_Pup-proteasome_system/5001905 DO - 10.6084/m9.figshare.5001905.v1 L4 - https://ndownloader.figshare.com/files/8423192 KW - proteolysis KW - Dop KW - Pup KW - PafA KW - proteasome KW - Stem Cells KW - Biochemistry KW - Molecular Biology KW - Developmental Biology KW - Structural Biology KW - Synthetic Biology KW - Proteomics and Intermolecular Interactions (excl. Medical Proteomics) KW - Evolutionary Biology KW - Signal Transduction KW - Cancer Cell Biology KW - Systems Biology KW - Bioinformatics KW - Heat and Mass Transfer Operations N2 - Pup, a ubiquitin analog, tags proteins for degradation by the bacterial proteasome. As an intracellular proteolytic system, the Pup-proteasome system (PPS) must be carefully regulated to prevent excessive protein degradation. Currently, those factors underlying PPS regulation remain poorly understood. Here, experimental analysis combined with theoretical modeling of in vivo protein pupylation revealed how the basic PPS design allows stable and controlled protein pupylation. Specifically, the recycling of Pup when targets are degraded allows the PPS to maintain steady state levels of protein pupylation and degradation at a rate limited by proteasome function, and at a pupylome level limited by Pup concentrations. This design allows the Pup-ligase, a highly promiscuous enzyme, to act in a controlled manner without causing damage, and the PPS to be effectively tuned to control protein degradation. This study thus provides understanding of how the inherent design of an intracellular proteolytic system serves crucial regulatory purposes. ER -