10. What are the steps involved in the ubiquitination of proteins? (select all that apply) a. E1 activates ubiquitin by hydrolyzing ATP to ADP and Pi to generate a thioester bond between ubiquitin C-terminus and an E1 Cysteine residue b. E1 activates ubiquitin by hydrolyzing ATP to AMP and PPI to generate a thioester bond between ubiquitin C-terminus and an E1 Cysteine residue c. E1 transfers activated ubiquitin to E2 enzymes through a transthioesterification reaction d. E2 enzymes directly add ubiquitin to substrate e. E2 enzymes directly add ubiquitin to HECT E3 Ligases f. E2 enzymes directly add ubiquitin to RING E3 Ligases g. E2 enzymes directly add ubiquitin to substrate bound to HECT E3 Ligases h. E2 enzymes directly add ubiquitin to substrate bound to RING E3 Ligases

Human Anatomy & Physiology (11th Edition)
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Author:Elaine N. Marieb, Katja N. Hoehn
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Chapter1: The Human Body: An Orientation
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10. What are the steps involved in the ubiquitination of proteins? (select all that apply)
a. E1 activates ubiquitin by hydrolyzing ATP to ADP and Pi to generate a thioester bond between
ubiquitin C-terminus and an E1 Cysteine residue
b.
E1 activates ubiquitin by hydrolyzing ATP to AMP and PPI to generate a thioester bond between
ubiquitin C-terminus and an E1 Cysteine residue
c. E1 transfers activated ubiquitin to E2 enzymes through a transthioesterification reaction
d. E2 enzymes directly add ubiquitin to substrate
e. E2 enzymes directly add ubiquitin to HECT E3 Ligases
f. E2 enzymes directly add ubiquitin to RING E3 Ligases
g. E2 enzymes directly add ubiquitin to substrate bound to HECT E3 Ligases
h. E2 enzymes directly add ubiquitin to substrate bound to RING E3 Ligases
11. How is ubiquitination regulated? (select all that apply)
a. Substrate selection for ubiquitination is mediated by E1 enzymes
b. Substrate selection for ubiquitination is mediated by E2 enzymes
c. Substrate selection for ubiquitination is mediated by E3 enzymes
d. Deubiquitinases act as 'erasers' of the ubiquitin posttranslational modification
e. Lysine residues of substrates can be protected from ubiquitination by being posttranslationally
modified by a different posttranslational modification
Transcribed Image Text:10. What are the steps involved in the ubiquitination of proteins? (select all that apply) a. E1 activates ubiquitin by hydrolyzing ATP to ADP and Pi to generate a thioester bond between ubiquitin C-terminus and an E1 Cysteine residue b. E1 activates ubiquitin by hydrolyzing ATP to AMP and PPI to generate a thioester bond between ubiquitin C-terminus and an E1 Cysteine residue c. E1 transfers activated ubiquitin to E2 enzymes through a transthioesterification reaction d. E2 enzymes directly add ubiquitin to substrate e. E2 enzymes directly add ubiquitin to HECT E3 Ligases f. E2 enzymes directly add ubiquitin to RING E3 Ligases g. E2 enzymes directly add ubiquitin to substrate bound to HECT E3 Ligases h. E2 enzymes directly add ubiquitin to substrate bound to RING E3 Ligases 11. How is ubiquitination regulated? (select all that apply) a. Substrate selection for ubiquitination is mediated by E1 enzymes b. Substrate selection for ubiquitination is mediated by E2 enzymes c. Substrate selection for ubiquitination is mediated by E3 enzymes d. Deubiquitinases act as 'erasers' of the ubiquitin posttranslational modification e. Lysine residues of substrates can be protected from ubiquitination by being posttranslationally modified by a different posttranslational modification
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