Multiple Choice
Before entering the proteasome the protein marked for degradation is unfolded.
6. Proteins
Protein Degradation
Struggling with Cell Biology?
Join thousands of students who trust us to help them ace their exams!Watch the first videoMultiple Choice
Which protein is responsible for attaching a ubiquitin molecule onto a protein to target it for degradation?
A
E1 ubiquitin activation enzyme
B
E2 ubiquitin conjugating enzyme
C
E3 ubiquitin ligase
D
E4 ubiquitin attachase
Verified step by step guidance1
Understand the ubiquitination process: Ubiquitination is a cellular mechanism that tags proteins for degradation by the proteasome. It involves a cascade of enzymatic activities.
Identify the roles of the enzymes involved: The ubiquitination process involves three main types of enzymes: E1, E2, and E3.
E1 ubiquitin-activating enzyme: This enzyme activates ubiquitin in an ATP-dependent manner, forming a high-energy thioester bond with ubiquitin.
E2 ubiquitin-conjugating enzyme: This enzyme receives ubiquitin from E1 and carries it to the E3 enzyme.
E3 ubiquitin ligase: This enzyme is responsible for transferring ubiquitin from the E2 enzyme to the target protein, thus tagging it for degradation. It provides specificity to the process by recognizing the substrate protein.
4:09mWatch next
Master Ubiquitin Proteasome Pathway with a bite sized video explanation from Kylia
Start learningRelated Videos
Related Practice
Protein Degradation practice set
Problem sets built by lead tutorsExpert video explanations