1)You add a drug to cells that can pass through hydrophilic or hydrobic environments (e.g., membranes & cytosol). The drug specifically prevents the binding of KDEL (ER retention signal) to any other molecules. In the short term, what would happen to the synthesis and localization of translocon proteins? a. New complete translocon proteins would be made, but they would end up in the golgi apparatus. b. New complete translocon proteins would be made, but they would end up at the plasma membrane c. No new intact translocon proteins would be synthesized d. New complete translocon proteins would be made, but they would be secreted e. New complete translocon proteins would be made and localized normally

1)You add a drug to cells that can pass through hydrophilic or hydrobic environments (e.g., membranes & cytosol). The drug specifically prevents the binding of KDEL (ER retention signal) to any other molecules. In the short term, what would happen to the synthesis and localization of translocon proteins? a. New complete translocon proteins would be made, but they would end up in the golgi apparatus. b. New complete translocon proteins would be made, but they would end up at the plasma membrane c. No new intact translocon proteins would be synthesized d. New complete translocon proteins would be made, but they would be secreted e. New complete translocon proteins would be made and localized normally

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter15: From Dna To Protein

Section: Chapter Questions

Problem 6TYK

See similar textbooks

Similar questions

A rare mutation can result in eukaryotic cells that causes a failure in the cell to synthesize the Signal Recognition Particle (SRP). Failure to make the SRP would impact protein synthesis by ________ . A. Preventing transition of bound ribosomes to free ribosomes B. Preventing binding of ribosomes to the rough ER during synthesis of proteins with a signal sequence C. Preventing export of mRNA out of the nuclear envelope D. Preventing binding of ribosomes to the smooth ER during synthesis of proteins with a signal sequence
As a researcher who studies cytoskeletal dynamics, you create a microtubule subunit that cannot hydrolyze GTP. How would the critical concentration for the minus end of a polymer formed by these mutant subunits compare to that of the minus end of a fiber formed by normal microtubule subunits? Why? How would the critical concentration for the minus end of a fiber formed by these mutant subunits compare to that of the plus end of a fiber formed by normal microtubule subunits? Why?
1. Which of the listed protein would NOT be expected to have experienced vesicular transport? A. Cis-golgi enzymes B. Proteins in early and late and endosomes due to pinocytosis C. Lysosomal enzymes D. A multi-pass transmembrane protein in the plasma membrane E. All of the above proteins Actually would undergo vesicular transport at some point 2. What would be the effect of COPI-coated vesicles if a cell is treated with GTP analogous that can bind the ARF G protein but can not trigger the exposure of its lipid anchor. A. They will decrease substantially in number in the cytoplasm B. They will accumulate in the nucleus C. They will fuse into one giant vesicle that was seen in the cytoplasm D. They will accumulate in the cytoplasm E. They will decrease substantially in number in the nucleus
Yeast cells are eukaryotes, and they require a functional secretory pathway to grow and to maintain cellular organization. But surprisingly, when SRP is removed from yeast cells by deleting the relevant genes, the cells are still alive (although they grow slowly). a) How can yeast survive without SRP? Propose two alternative hypotheses. b) How might electron microscopy of normal and SRP-deficient yeast cells help you to distinguish between these two hypotheses?
You genetically engineered a cell to no longer contain the extracellular domain of an integrin. What is the most likely effect of losing this domain on the cell's ability to bind? A It would affect the cell's ability to attach to the ECM. B It would have no effect on the cell's ability to attach to anything. C It would affect the cell's ability to attach to the cytoskeleton through adaptor proteins. D It would affect both the cell's ability to attach to other cells and the cell's ability to attach to the cytoskeleton.
Eukaryotic cells manufacture cytoskeletal proteins, which help to maintain cell shape and function. What would you predict about these proteins? A. They initially contain signal sequences that allow their entrance into the endoplasmic reticulum B. They are glycosylated in the Golgi apparatus C. They travel to the nucleus in a transport vesicle with a specific signal D. They are manufactured on free ribosomes in the cytoplasm
The site of translation is the a) nucleus b) ribosomes c) lysosomes d) mitochondria Which of these pairs of molecules dissolved in water not produce a buffer solution? a) HF and NaF b) NH3 and NH4Cl c) CH4 and H2O d) NaH2PO4 and Na2HPO4 The soap-water-oil mixture that you made in your amphipathic home lab exercise may be best described as: a) an amphipathic substance b) a hydrophilic substance c) a hydrophobic substance d) an emulsion Which of these amino acids would have a negative charge at pH 7.0? a) Lys b) Asp c) Met d) Gly Which of these amino acids has two nitrogen atoms in its structure? a) Lys b) Arg c) Tyr d) Val Beta sheets are an example of: a) primary structure b) secondary structure c) tertiary structure d) quaternary structure Folding in myoglobin are an example of: a) primary structure b) secondary structure c) tertiary structure d) quaternary structure
What is the primary characteristic of peripheral membrane proteins? A: They cannot be post-translationally modified. B: They span the entire lipid bilayer, sometimes multiple times. C: Detergents or nonpolar solvents are necessary to remove them from the lipid bilayer. D:Weak intermolecular forces keep them attached to the lipid membrane.
You are investigating the transport of proteins into the ER in various mutant cells. Where would you expect to find ER proteins in a cell in which the gene encoding TOM proteins have been knocked out? a. Proteasome b. Cytoplasm c. Mitochondria d. nucleus e. ER
A useful technique for studying microtubule motors is to attach them by their tails to a glass coverslip (which can be accomplished quite easily because the tails stick avidly to a clean glass surface) and then allow them to settle. The microtubules may then be viewed in a light microscope as they are propelled over the surface of the coverslip by the heads of the motor proteins. Because the motor proteins attach at random orientations to the coverslip, however, how can they generate coordinated movement of individual microtubules rather than engaging in a tug-of-war? In which direction will microtubules crawl on a ‘bed’ of kinesin molecules (i.e., will they move plus-end first, or minus-end first)?
Why do cancer cells treated with vitamin E succinate appear to be more vulnerable to rupture of their lysosomal membranes (and subsequent apoptosis) than normal cells? A. cancer cells often have an alkaline cytosol, which destabilizes the acidic lysosomes B. cancer cells often have an alkaline cytosol, which destabilizes the alkaline lysosomes C. cancer cells often have an acidic cytosol, which destabilizes the acidic lysosomes D. cancer cells often have an acidic cytosol, which destabilizes the alkaline lysosomes E. all of the above
The following are steps that occur when a protein is targeted for synthesis on the endoplasmic reticulum (ER). Which of the following indicates the correct sequence for the signal mechanism that targets proteins for the ER? The SRP leaves and polypeptide synthesis resumes, with simultaneous translocation across the membrane. Polypeptide synthesis begins on a free ribosome in the cytosol. An SRP binds to the signal peptide, halting synthesis momentarily. The rest of the completed polypeptide leaves the ribosome and folds into its final conformation. The SRP binds to a receptor protein in the ER membrane that is part of a protein complex that forms a pore. The signal peptide is cleaved by an enzyme in the receptor protein complex. A. 2, 3, 5, 1, 6, 4 B. 2 ,3, 5, 6, 1, 4 C. 3, 1, 6, 5, 2, 4 D. 3, 2, 1, 5, 6, 4