Choose the statement that best describes how proteins move between different compartments within the secretory and endocyticpathways.O A. proteins exit their primary location via translocators and are transported to their next destination by SRPB. proteins are directly translated into the cellular compartment that will serve as their final destinationO C. proteins are packaged in vesicles that bud out of one membrane and fuse with the membrane at the next destinationO D. proteins diffuse through the membrane where they originated and are bound by chaperones who transport them to their nextdestination

Proteins are sorted in the Golgi and delivered to cell membrane, lysosomes or storage granules.…

Answered: ose the statement that best describes…

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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Similar questions

While studying the secretory pathway, you make the following observation about proteins destined for the ER: Proteins translated in vitro in the absence of microsomes migrate more slowly on an SDS PAGE gel than those translated in the presence of microsomes. What might account for the observed protein size difference? A. SRP, present only in microsomes, and binds to and removes the signal sequence from the protein, resulting in a protein is smaller and migrates more quickly on a gel. B. Signal peptidase, present only in the microsomes, cleaves the signal sequence from the protein, making the protein smaller and therefore migrate more quickly. C. In vitro translated proteins tend to be larger due to a more stable poly A tail D. Signal peptidase, present only in the microsomes, adds a signal sequence to the protein, making the protein larger and therefore migrate more slowly.
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?
What is the fate of an acid hydrolase that does not get tagged with mannose-6-phosphate in the Golgi? A. returned to the ER B. secreted out of the cell C. transported to the lysosome O D. degraded by the proteasome
Where do antibiotics such as penicillin, amoxicillin, vancomycin, and cephalosporins exert their action on bacterial cells? Group of answer choices inhibit protein synthesis at the ribosome break sugar-bonds between NAGs and NAMs inhibit cell membrane formation inhibit protein cross-links
The process by which messenger RNA codes for the synthesis of a specific protein is called: a) replication b) transcription c) translation d) gene regulation Which statement is true about prokaryotes? A) they have no chromosomes b) they have chromosomes, but they are not membrane bound c) they have membrane bound chromosomes d) their chromosomes are made of RNA rather than DNA In a eukaryotic cell, most ATP is made in which location? A) nucleus b) mitochondria C) cytoplasm d) golgi apparatus
1) Which of the following contains all of the information required to target a precursor protein from the cytosol to the mitochondrial matrix? a. N-terminal uptake-targeting sequence b. C-terminal uptake-targeting sequence c. post-translational organelle d. translocon e. None of the above 2) In the absence of targeting information, what is the default location of proteins synthesized on cytosolic ribosomes? a. Golgi apparatus b. ER lumun c. Cytosol d. Cell plasma membrane e. ER membrane
What structural characteristics of mucopolysaccharides facilitate the removal of pathogens? A. Mucopolyssacharides contain many negatively charged groups, which can interact with positively charged proteins. B. Mucopolysaccharides have hydrophilic groups that can interact with large amounts of water and accommodate these in flexible structures facilitating excretion from the cell. C. Mucopolysaccharides have flexible structures because these are not covalently linked in proteoglycans. D. Both A. and B. E. All of these.
Consider two different proteins that are leaving from the Golgi in order to arrive in their common destination, a lysosome. In order for these two different proteins to be sent to the same place, what should they have in common? A) They must have the same primary structure B) They must have been imported into the cell by endocytosis. C) They must have the same tertiary structure D) They probably have the same glycosylation pattern. ..
In cell culture experiments, when you add the puriﬁed toxin to host cell monolayers, the host cells die. The toxin-infected host cells do not lyse, but the cells have collapsed and show a signiﬁcant loss of water and ions. The toxin is translated and produced by the bacterium as a single polypeptide. However, cellular fractionation of the host cells into cytosolic and membrane fractions reveals that a portion of the toxin is present in the membrane fraction and another portion is in the cytosolic fraction. Based on these results, answer the following questions: A. What type of toxin have you identiﬁed? 2 B. How does this toxin function to kill host cells?
In eukaryotic cells secreted proteins are targeted first to the endoplasmic reticulum and then pass through the Golgi, before being released from secretory vesicles into the extracellular space. A much simpler route would be for ribosomes synthesising secretory proteins to be targeted to a translocon in the plasma membrane, with the protein being secreted directly as it is translated. List three potential advantages of the former, more circuitous, route for protein secretion over the simpler, more direct, alternative route suggested.
12. Which statement regarding cell-surface receptors is correct? A) lon-channel-coupled receptors alter the membrane potential directly by changing the permeability of the plasma membrane. B) G-protein-coupled receptors are polypeptides with seven transmembrane domains. C) After binding their ligand, G-protein-coupled receptors interact with intracellular GTP-binding proteins, later initiating signal transduction events. D) All of the above E) None of the above Answer: Explanation:
The studies of Palade and colleagues used pulse chase labeling with radioactively labeled amino acids and auto radiography to visualize the location of newly synthesized proteins in pancreatic acinar cells. These early experiments provided invaluable information on protein synthesis and intercompartmental transport. New methods have replaced these early approaches, but two basic requirements are still necessary for any assay to study this type of protein transport. What are they, and how do recent experimental approaches meet these criteria?

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