The regulatory significance of tag recycling in the mycobacterial Pup-proteasome system.

Autor: Elharar Y; Department of Life Sciences, Ben-Gurion University of the Negev, Beer-Sheva, Israel., Schlussel S; Department of Life Sciences, Ben-Gurion University of the Negev, Beer-Sheva, Israel., Hecht N; Department of Life Sciences, Ben-Gurion University of the Negev, Beer-Sheva, Israel., Meijler MM; Department of Chemistry, Ben-Gurion University of the Negev, Beer-Sheva, Israel.; The National Institute for Biotechnology in the Negev, Ben-Gurion University of the Negev, Beer-Sheva, Israel., Gur E; Department of Life Sciences, Ben-Gurion University of the Negev, Beer-Sheva, Israel.; The National Institute for Biotechnology in the Negev, Ben-Gurion University of the Negev, Beer-Sheva, Israel.
Jazyk: angličtina
Zdroj: The FEBS journal [FEBS J] 2017 Jun; Vol. 284 (12), pp. 1804-1814. Date of Electronic Publication: 2017 May 18.
DOI: 10.1111/febs.14086
Abstrakt: 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.
(© 2017 Federation of European Biochemical Societies.)
Databáze: MEDLINE
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