Why is proteasome degradation of poly-ubiquitylated proteins so energetically expensive? Unfoldase does not easily denature stable proteins with each round of ATP hydrolysis O The ubiquitin receptor in the proteasome cap requires multiple ATP units to bind to the substrate Attaching each ubiquitin requires the release of two phosphates from ATP E3 ubiquitin ligases require many rounds of ATP hydrolysis to transfer the ubiquitin to the substrate O Each ubiquitin has to be removed before the protein can be degraded

Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
Section: Chapter Questions
Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...
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**Question: Why is proteasome degradation of poly-ubiquitylated proteins so energetically expensive?**

- Unfoldase does not easily denature stable proteins with each round of ATP hydrolysis
- The ubiquitin receptor in the proteasome cap requires multiple ATP units to bind to the substrate
- Attaching each ubiquitin requires the release of two phosphates from ATP
- E3 ubiquitin ligases require many rounds of ATP hydrolysis to transfer the ubiquitin to the substrate
- Each ubiquitin has to be removed before the protein can be degraded
Transcribed Image Text:**Question: Why is proteasome degradation of poly-ubiquitylated proteins so energetically expensive?** - Unfoldase does not easily denature stable proteins with each round of ATP hydrolysis - The ubiquitin receptor in the proteasome cap requires multiple ATP units to bind to the substrate - Attaching each ubiquitin requires the release of two phosphates from ATP - E3 ubiquitin ligases require many rounds of ATP hydrolysis to transfer the ubiquitin to the substrate - Each ubiquitin has to be removed before the protein can be degraded
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