You are working in the lab, with a cell-free translational system that contains microsomes. Microsomes are artificial structures derived from pieces of endoplasmic reticulum (ER) formed during tissue homogenization. These microsomes lack the signal recognition particle or SRP. You translate an mRNA that codes for a secretory protein using this system. Which of the following outcomes do you expect? The protein will be synthesized and its signal sequence will be removed O The protein will be synthesized and will be incorporated into the microsome O No protein synthesis O The protein will be synthesized and will not be incorporated into the microsome

You are working in the lab, with a cell-free translational system that contains microsomes. Microsomes are artificial structures derived from pieces of endoplasmic reticulum (ER) formed during tissue homogenization. These microsomes lack the signal recognition particle or SRP. You translate an mRNA that codes for a secretory protein using this system. Which of the following outcomes do you expect? The protein will be synthesized and its signal sequence will be removed O The protein will be synthesized and will be incorporated into the microsome O No protein synthesis O The protein will be synthesized and will not be incorporated into the microsome

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Description: You are working in the lab, with a cell-free translational system that containsmicrosomes. Microsomes are artificial structures derived from pieces of endoplasmicreticulum (ER) formed during tissue homogenization.These microsomes lack the signal rec

BIOLOGY:CONCEPTS+APPL.(LOOSELEAF)

10th Edition

ISBN:9781305967359

Author:STARR

Publisher:STARR

Chapter9: From Dna To Protein

Section: Chapter Questions

Problem 15SA: Put the following processes in order of their occurrence during expression of a eukaryotic gene: a....

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In eukaryotic cells, secreted proteins are initially directed to the endoplasmic reticulum and then via the Golgi, where they are released into the extracellular environment through secretory vesicles. A more easier way would be for secretory protein-producing ribosomes to be localised to a translocon in the plasma membrane, with the protein being secreted directly during translation. Consider three possible benefits of the more roundabout method for protein secretion versus the simpler, more straightforward approach indicated.
Imagine that you are working with DNA sequences of soluble proteins (not membrane proteins) and have the technology to genetically engineer/alter the existing sequence and you can express this particular protein in a yeast cell model. You also have the power to track and visualize where the genetically engineered proteins traffic in your model system. You engineer an ER signal sequence to the amino-terminal end of a normally cytosolic protein. Which best describes the fate of this protein? The protein is degraded The protein remains in the cytosol The protein is translocated through the ER membrane translocon channel, N' end first The protein is translocated through the ER membrane translocon channel, C' end first
Gene X codes for a protein in eukaryotes. A mutated eukaryotic cell contains an altered base-pair in an intron of gene X. Which would be the most likely effect of this mutation on the biomolecules in the cell? The amount of pre-mRNA transcribed from gene X would be less than normal. The amount of functional protein corresponding to gene X would be less than normal. The ability of snRNAs to form a spliceosome would be diminished. The breakdown of mature mRNA corresponding to gene X would be faster
You are working on a protein for a research project. The protein does not express well in prokaryotic expression systems so you decide to try a eukaryotic system, baker’s yeast, instead. As part of the expression system, you add a signal peptide to the protein so that it will be exported through the endomembrane system to the outside of the yeast cell. This makes purifying the protein much simpler. During the purification, you notice that the protein is heavier than it should be during gel filtration chromatography. This is confirmed by SDS-PAGE. What could be the reason that the protein has gained mass when expressed in the eukaryotic system?
The following is the only intron sequence of a gene that will be excised during the maturation of the mRNA. But it is not spliced in some tissues, where alternative splicing pattern is seen. Will the amino acid of its protein product following this sequence change? Explain with an example. ATGATAGCCAGACTCGCA
Protein X is a secretory protein that is synthesized on ER-bound polyribosomes in vivo. You synthesized this protein in an in-vitro protein translation system in the absence of microsomes. You add microsomes post-translationally to this system. What do you expect to see? Group of answer choices The signal sequence of the protein will be cleaved off The protein will be translocated across the microsomal membrane. The protein will be sensitive to the action of proteases The protein will be glycosylated All of the answer choices are correct
The Iron Response Factor (IRF) protein regulates production of both the iron transport protein transferrin, which imports iron into a cell, and the iron storage protein ferritin, which stores iron when the cell has more iron than in needs. IRF is an RNA binding protein, which binds to a specific RNA sequence, the Iron Response Element (IRE). When the IRF protein binds to the IRE sequence in the mRNA that codes for transferrin, what effect does this have on the expression of transferrin? Briefly explain why this effect is observed.
A protein complex in the nucleus is responsible for transporting mRNA molecules into the cytoplasm. Describe the proteins that form this exporter. What two protein groups are probably behind the mechanism involved in the directional movement of the mRNP and exporter into the cytosol?
Imagine the same cells as above that has 20,000 molecules of estrogen receptor at the start of your experiment. You treat the cell with alpha amanitin, but forgot to add cycloheximide. The steady state level of estrogen receptor mRNA transcripts in the cell is 200. Ecah transcript takes two minutes to be translated into estrogen receptor protein. Assuming none of the ER mRNAs in the cell decay during the course of the experiment, at your 1 hour time limit, how many ER proteins will be present in the cell treated with only alpha aminitin?
Imagine that you are working with DNA sequences of soluble proteins (not membrane proteins) and have the technology to genetically engineer/alter the existing sequence and you can express this particular protein in a yeast cell model. You also have the power to track and visualize where the genetically engineered proteins traffic in your model system. You engineer an ER signal sequence to the carboxyl-terminal end of a normally cytosolic protein. Which best describes the fate of this protein? O The protein is translocated through the ER membrane translocon channel, N' end first O The protein is translocated through the ER membrane translocon channel, C' end first The protein is degraded The protein remains in the cytosol
Put the following processes in order of their occurrence during expression of a eukaryotic gene: a. mRNA processing c. transcription b. translation d. RNA leaves nucleus
You are studying how gene expression is regulated in the cell. For gene z, you find that while there are high levels of mRNA in the cell, there are low levels of the protein encoded by gene z. Describe a regulatory mechanism that could explain this finding that occurs after translation.