Biochemistry : Ubiquitination Pathway
Study concepts, example questions & explanations for Biochemistry
All Biochemistry Resources
Example Questions
Example Question #1 : Protein Degradation
If a protein is bonded to ubiquitin, this tells the cell that the protein should be __________.
inactivated
degraded
elongated
shortened
activated
degraded
When a protein is damaged, it can be tagged with the molecule, ubiquitin. This signals to the cell that the protein is no longer functioning properly and needs to be degraded.
Example Question #1 : Ubiquitination Pathway
HMGCoA reductase (3-hydroxy-3-methyl-glutaryl-CoA reductase) is the rate-limiting enzyme in cholesterol synthesis. Which of the following are true about the ubiquitination of this enzyme?
I. When cholesterol levels in the cell are high, the reductase binds to insulin-induced gene 1 proteins.
II. Binding to insulin induced gene 1 proteins leads to ubiquitination and proteasomal degradation of reductase.
III. Ubiquitination occurs through the binding of the C-terminal glycine of ubiquitin to the amino group of a lysine on the reductase.
IV. The enzyme tagged with ubiquitin is recognized by the proteasome where proteolysis occurs.
II and III
I and II
I, II, III, and IV
II and IV
II, III, and IV
I, II, III, and IV
HMGCoA reductase is the rate-limiting enzyme in cholesterol synthesis. The reductase is present on the endoplasmic reticulum membrane. When levels of its product, cholesterol, are high, the enzyme gets ubiquitinated and degraded in smaller peptides and amino acids. It first binds to insulin-induced gene 1 protein before ubiquitination.
All Biochemistry Resources
