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- W2296163025 abstract "Significance This work describes how a basic regulatory challenge, namely the balancing of two opposing activities of a single enzyme while coordinating these actions with the activity of another enzyme, is addressed in a biological system. In the Pup-proteasome system, the bacterial parallel of the ubiquitin-proteasome system, Pup modification by Dop (deamidase of Pup) is a prerequisite for pupylation by proteasome accessory factor A. Paradoxically, Dop also reverses pupylation through its ability to depupylate substrates. We show that this challenge is resolved posttranslationally by combining substrate discrimination based on molecular weight, and by regulating enzyme levels in response to external stimuli. These findings provide an example of how directionality and coordination of enzyme activities in a single pathway are regulated according to physiological requirements of the cell." @default.
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- W2296163025 date "2016-03-07" @default.
- W2296163025 modified "2023-09-30" @default.
- W2296163025 title "Posttranslational regulation of coordinated enzyme activities in the Pup-proteasome system" @default.
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- W2296163025 doi "https://doi.org/10.1073/pnas.1525185113" @default.
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