ERAD, or ER associated degradation, is a quality control measure with the following function: O A. misfolded proteins activate the expression of genes such as chaperones that will help to refold and stabilize misfolded proteins until the fold correctly O B. proteins that cannot fold correctly are ejected from the ER through the translocon and degraded by the ubiquitin-proteasome system in the cytosol OC. misfolded proteins are ubiquitinated and degraded by proteasomes inside the ER O D. Unfolded proteins in the ER activate a transmembrane kinase in the ER that phosphorylates misfolded proteins that are sent to the lysosome in vesicles for degradation

ERAD, or ER associated degradation, is a quality control measure with the following function: O A. misfolded proteins activate the expression of genes such as chaperones that will help to refold and stabilize misfolded proteins until the fold correctly O B. proteins that cannot fold correctly are ejected from the ER through the translocon and degraded by the ubiquitin-proteasome system in the cytosol OC. misfolded proteins are ubiquitinated and degraded by proteasomes inside the ER O D. Unfolded proteins in the ER activate a transmembrane kinase in the ER that phosphorylates misfolded proteins that are sent to the lysosome in vesicles for degradation

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter9: Gene Expression And Gene Regulation

Section: Chapter Questions

Problem 18QP: The following is a portion of a protein: met-trp-tyr-arg-gly-pro-thr-Various mutant forms of this...

See similar textbooks

Similar questions

Many neurodegenrative diseases are thought to be caused by increased levels of unfolded proteins. Which of the following conditions would you expect to increase unfolded protein levels (select all that apply)? A. Reduced expression of chaperone proteins B. A mutation that inactivates the proteasome C. Increased levels of ubiquitin D. Inactivating mutation in ubiquitin ligase, an enzyme necessary for attaching ubiquitin to proteins in cytosol E. Mutation of N-terminal amino acid from Methionine to Arginine
The following is a portion of a protein: met-trp-tyr-arg-gly-pro-thr-Various mutant forms of this protein have been recovered. Using the normal and mutant sequences, determine the DNA and mRNA sequences that code for this portion of the protein, and explain each of the mutations. a. met-trp- b. met-cys-ile-val-val-leu-gln- c. met-trp-tyr-arg-ser-pro-thr- d. met-trp-tyr-arg-gly-ala-val-ile-ser-pro-thr-
In the ubiquitin-proteasome pathway of degradation, what component is most important in determining specificity when selecting proteins for destruction? a)ubiquitin b)E1 ubiquitin-activating enzyme c)E2 ubiquitin-conjugating enzyme d)E3 ubiquitin-protein ligase e)19S proteasome
Like Hurler syndrome, Fabry disease involves an abnormal accumulationof substances within lysosomes. However, the lysosomesof individuals with Fabry disease show an abnormal accumulationof lipids. The defective enzyme is α-galactosidase A, which is alysosomal enzyme that functions in lipid metabolism. The enzymaticdefect causes cell damage, especially to the kidneys, heart,and eyes. The gene that encodes α-galactosidase A is found on theX chromosome. Let’s suppose a phenotypically unaffected coupleproduces two sons with Fabry disease and one phenotypicallyunaffected daughter. What is the probability that the daughter willhave an affected son?
Which of the following statements regarding O-linked glycosylation is FALSE? A. It occurs on asparagines (Asn) in specific proteins. B. It is an important post-translational protein modification. C. It is built sequentially on proteins by individual enzymes that are found in each cisterna of the Golgi (i.e. cis, medial, trans). D. It occurs in the Golgi. It occurs on serine (Ser) and threonine (Thr) residues in specific proteins.
If lactose is present in a cell with the following genotype, will functional Beta – galactosidase and/or permease be made? LacIs, LacP+, LacOc, LacZ+, LacY- / LacI+, LacP+, LacO+, LacZ-, LacY+ Group of answer choices Both genes will make functional protein. Only Beta – galactosidase will be functional. Only permease will be functional. No functional proteins will be made.
What is a hydropathy plot, and why is it used?A.A hydropathy plot, is a graph showing the distribution of hydrophobic amino acids along the length of a peptide sequence and is used to predict the regions within a protein most likely to be post-translationally modified with a lipid moiety. B.A hydropathy plot identifies the concentration of water in a cell and is used to predict the type of metabolic reactions performed by the cells. C.A hydropathy plot , is a graph showing the distribution of hydrophillic amino acids along the length of a peptide sequence and is used to predict the regions within a protein most likely to be glycosylated. D.A hydropathy plot, is a graph showing the distribution of hydrophobic amino acids over the length of a paptide sequence, which is used to predict the position of transmembrane domains within a protein.
The following quote is from a TiBS review article (Y. Shiloh,(2006) TiBS vol. 31 No7 Pages 402-410). Please explain what information would have been derived from genetics experiments and what information would have been based on biochemistry experiments. Explain how using both genetic and biochemistry has allowed us to greatly enhance our understanding of this field. ATM belongs to a conserved family of proteins termed the ‘PI3K-like protein kinases’( PIKKs), most of which possess a serine/threonine kinase activity and all of which, as their name indicates, contain a domain with motifs that are typical of the lipid kinase phosphatidylinositol3- kinase(PI3K) [39]. At present, the mammalian members of this family include five protein kinases: ATM, ataxia-telangiectasia- and Rad3-related (ATR), hSMG-1, mTOR (also known as FRAP) and the catalytic subunit of the DNA-dependent protein kinase (DNA-PK). Another member of the PIKK family is TRRAP, a protein component of histone…
Describes a method known as Western blotting that can be used to detect a polypeptide that is translated from a particular mRNA. In this method, a particular polypeptide or protein is detected by an antibody that specifically recognizes a segment of its amino acid sequence. After the antibody binds to the polypeptide within a gel, a secondary antibody (which is labeled) is used to visualize the polypeptide as a dark band.For example, an antibody that recognizes α-galactosidase A couldbe used to specifically detect the amount of α-galactosidase A proteinon a gel. The enzyme α-galactosidase A is defective in individuals with Fabry disease, which shows an X-linked recessive pattern of inheritance. Amy, Nan, and Pete are siblings, and Pete has Fabry disease. Aileen, Jason, and Jerry are brothers and sister, and Jerry has Fabry disease. Amy, Nan, and Pete are not related to Aileen, Jason, and Jerry. Amy, Nan, and Aileen are concerned that they could be carriers of a defective…
Protein transfer to a membrane from a developed electrophoretic gel can be performed under which of the following conditions?
Place the steps below in the correct order to accurately reflect the steps by which a secretory protein is co-translationally imported into the lumen of the endoplasmic reticulum: As the polypeptide elongates and translocates into the ER, the signal peptidase cleaves the signal peptide. The SRP binds the SRP receptor, directing the ribosome to dock on the ER membrane. Termination of translation, results in the release of the polypeptide into the ER lumen, release of the ribosome from the ER membrane, and closing of the channel. The signal recognition particle (SRP) binds to the signal sequence on a newly synthesized polypeptide and stalls translation. The channel in the ER membrane opens and the polypeptide is inserted into the ER lumen. The SRP is released. A.6-4-2-3-1-5 B.4-2-5-1-3-6 C.3-1-6-2-4-5 D.1-2-3-4-5-6 E.2-6-1-5-4-3
Numerous diseases are treated by injection of polypeptide growth factors, such as human growth factor. A project team in a pharmaceutical company wishes to produce high levels of a growth factor for therapeutic use by overexpressing and purifying the protein from E coli. The team takes the cDNA of the human gene and makes the mutations below before transferring the gene to E coli for high level protein expression. As seen in the gel below, the mutations dramatically enhanced the levels of protein produced (growth factor indicated by arrows). Explain why the team altered the human cDNA of the growth factor as shown below for expression in E coli (limit 3-4 sentences).