14. Question What happens to ubiquitin after the protein is unfolded? It is degraded with the protein. It returns to the nucleus. It is recycled. It synthesizes new proteins.
Added by Emilio W.
Close
Step 1
It tags proteins that are destined for destruction. Show more…
Show all steps
Your feedback will help us improve your experience
Adi S and 70 other Biology educators are ready to help you.
Ask a new question
Labs
Want to see this concept in action?
Explore this concept interactively to see how it behaves as you change inputs.
Key Concepts
Recommended Videos
Pre-Lecture Question Which of the following describes the action of the 26S proteasome on ubiquitin-tagged proteins? Both ubiquitin and its linked protein are degraded to amino acids, in an ATP-dependent fashion. Both ubiquitin and its linked protein are degraded to peptides of about residues, in an ATP-dependent fashion. Both ubiquitin and its linked protein are degraded to amino acids, in an ATP-independent fashion. The linked protein, but not ubiquitin, is degraded to peptides of about residues in an ATP-dependent fashion.
Adi S.
1) Why don't all proteins with a ubiquitin chain get degraded by the proteasome? 2) What other outcomes might occur for a ubiquitin-tagged protein? 3) What are the basic structural, organizational, and functional features of the nucleus?
If you attach one and only one ubiquitin molecule to each of the three lysine residues of a cytoplasmic protein, where will the protein be sorted to (nucleus, proteasome, endosome/MVB/lysosome, none of the above)?
Recommended Textbooks
Biology for AP Courses
Objective Biology for NEET
Introduction to General, Organic and Biochemistry
Transcript
18,000,000+
Students on Numerade
Trusted by students at 8,000+ universities
Watch the video solution with this free unlock.
EMAIL
PASSWORD