Prescott's Microbiology
11th Edition
ISBN: 9781260211887
Author: WILLEY, Sandman, Wood
Publisher: McGraw Hill
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Textbook Question
Chapter 17.4, Problem 4CC
You are studying
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
Rho independent terminators
Select an answer and submit. For keyboard navigation, use the up/down arrow keys to select an answer.
a
a) contain a GC rich stem loop followed by a run of Us
b
b) need the help of other proteins to terminate transcription
C) are very rare in E. coli
d) none of the above
A newly identified protein from the cells of the Panopyra plant on Pandora was shown to inhibit translation of its target genes by binding to the 5’ UTR of the mRNA and preventing ribosome binding. A possible way this inhibition may be relieved by an sRNA would be:
Group of answer choices
a)The sRNA acts as a silencer, suppressing the inhibitory protein and allowing translation to take place.
b)The sRNA acts as a decoy, sequestering the inhibitory protein and allowing translation to take place.
c)The sRNA acts as a marker, flagging the inhibitory protein for ubiquitination and allowing translation to take place.
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
The protein will be synthesized and will be incorporated into the microsome
O No protein synthesis
The protein will be synthesized and will not be incorporated into the microsome
Chapter 17 Solutions
Prescott's Microbiology
Ch. 17.1 - Examine the uncut piece of DNA shown in the upper...Ch. 17.1 - Which of the above enzymes yield blunt ends? Which...Ch. 17.1 - Prob. 3MICh. 17.1 - What would you conclude if you obtained only blue...Ch. 17.1 - Why must introns be removed from eukaryotic DNA...Ch. 17.1 - Which plasmid is a shuttle vector? Why?Ch. 17.1 - In what ways does the BAC shown here differ from...Ch. 17.1 - Describe restriction enzymes, sticky ends, and...Ch. 17.1 - What is cDNA? Why is it necessary to generate cDNA...Ch. 17.1 - Prob. 3CC
Ch. 17.1 - Prob. 4CCCh. 17.1 - Prob. 5CCCh. 17.2 - Why, after three cycles, are the vast majority of...Ch. 17.2 - Briefly describe the polymerase chain reaction....Ch. 17.2 - Why is PCR used to detect infectious agents that...Ch. 17.2 - How would you use PCR to measure the concentration...Ch. 17.2 - Why is it possible to visualize a PCR product on...Ch. 17.2 - Prob. 5CCCh. 17.3 - Why are long fragments (e.g., 20,000 bp) of...Ch. 17.4 - What special considerations are necessary if one...Ch. 17.4 - Prob. 1CCCh. 17.4 - Prob. 2CCCh. 17.4 - Prob. 3CCCh. 17.4 - You are studying chemotaxis proteins in a newly...Ch. 17.5 - Prob. 1MICh. 17.5 - Prob. 1CCCh. 17.5 - Prob. 2CCCh. 17 - Which of the DNA molecules shown are recombinant?Ch. 17 - Prob. 1RCCh. 17 - Prob. 2RCCh. 17 - Prob. 3RCCh. 17 - Prob. 4RCCh. 17 - Prob. 5RCCh. 17 - Prob. 6RCCh. 17 - Prob. 1ALCh. 17 - Prob. 2ALCh. 17 - Suppose you transformed a plasmid vector carrying...Ch. 17 - You are interested in the activity and regulation...Ch. 17 - Prob. 5ALCh. 17 - Prob. 6ALCh. 17 - Prob. 7AL
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- General transcription factors Select an answer and submit. For keyboard navigation, use the up/down arrow keys to select an answer. a a) act at every gene for a given RNA pol b b) act only at specific genes for under specific conditions c) must be very close to the promoter C d) none of the abovearrow_forwardYou have created a green fluorescent protein (GFP) fusion to a protein that is normally secreted from yeast cells. Because you have learned about the use of temperature-sensitive mutations in yeast to study protein and vesicle transport, you obtain three mutant yeast strains, each defective in some aspect of the protein secretory process. Being a good scientist, you of course also obtain a wild-type control strain. You decide to examine the fate of your GFP fusion protein in these various yeast strains and engineer the mutant strains to express your GFP fusion protein. However, in your excitement to do the experiment, you realize that you did not label any of the mutant yeast strains and no longer know which strain is defective in what process. You end up numbering your strains with the letters A to D, and then you carry out the experiment anyway, obtaining the results shown in the figure below (the black dots represent your GFP fusion protein). strain A strain B strain C strain D…arrow_forwardWhat is a possible outcome of the addition of a transcription factor such as Myod to the nucleus of a cell? Assume that there are no other factors to either activate or prevent the response of the cell. Group of answer choices A) Production of mRNA from genes that were previously not expresed B)adding methyl groups to DNA C)prevention of protein synthesis D)uncoiling of the chromatin to allow transcriptionarrow_forward
- Expression of a gene, in terms of greater production of the protein it encodes, could be increased by ... Question 12 options: A) increasing transcription of that gene. B) inhibiting proteases that break down the protein it encodes C) increasing the half life of its mRNA transcript D) A and C E) A, B and Carrow_forwardA scientist engineered a set of genes, each encoding a protein with two conflicting signal sequences. If the genes were expressed in a cell, predict which signals are preferred to be used and explain your choices. The sequence: a) C-terminal, signal for import into nucleus, signal for import into ER, N-terminal. b) C-terminal, signal for retention in ER, signal for import into mitochondria, N-terminal. c) Has signal for import into nucleus and signal for export from nucleus.arrow_forwardYou plan to synthesize a peptide to be used as a vaccine to treat melanoma, a particularly aggressive form of skin cancer. Normally, gp100, a protein on the surface of melanocytes, activates cell growth when it is bound by its ligand. Activation of the growth pathway depends on the presence of threonine in the ligand. The effective peptide vaccine will mimic the natural ligand, but won’t cause cell growth and division. Below is the sequence of the natural ligand: LDMKTAG In order to ensure your newly designed peptide vaccine does not cause cell growth upon binding, you must substitute the Threonine residue at position 5. What amino acid would you replace it with, bearing in mind that the peptide should still be similar enough to bind to the gp100 protein in the surface of melanocytes. Explain your choice. Your vaccine will be administered as a topical cream, and you require your peptide to have an overall neutral charge in order to be functional. At what pH should you formulate…arrow_forward
- You are interested in studying a novel gene that appears to be involved in cancer. There is no information about the function of this gene. What would you do to obtain the cDNA for this gene? How would you express this gene and what expression systems might you utilize to study its function and why? How would determine the subcellular localization of this gene in eukaryotic cells? What are alternative methods in case one doesn't work? How would you purify and determine the 3-dimensional structure of this protein?arrow_forwardATM is a kinase that phosphorylates histone H2AX in response to double-stranded DNA breaks. Which of the following scenarios would most quickly regulate ATM activity in the cell? a) Adding silencing methyl groups to cytosines in the Atm gene b) Modifying the histone code for the Atm gene c) Increasing expression of a miRNA specific for the Atm mRNA d) Activating an E3 ubiquitin ligase specific for the ATM proteinarrow_forwardi)Describe attenuation control and how it is used to regulate gene expression. ii)Give a specific example of how this works? iii)Could this be used in eukaryotes? why ?or why not?arrow_forward
- Gene Expression: 14) Look at the diagram: a) For each of the molecules in the diagram, identify what type of molecule they are, and label their ends (3',5',N,C). b) For each arrow, name the process and identify the major enzymes involved. c) Where do each of these activities take place in a bacterial cell? In a eukaryotic cell? Draw a picture if it helps you explain it.arrow_forwardProvide a detailed description of gene expression and control in prokaryotes. Provide a detailed description of proteins critical for this process. (please hand draw a figure showing gene expression and control in prokaryotes and the proteins involved)arrow_forwardThe amino acid asparagine is synthesized from aspartic acid by the enzyme asparagine synthetase (AS). In the previous problem you proposed a model for how this gene could be regulated. Suppose that you carry out an experiment to test your model. To do this you cut out the regulatory sequences upstream of the gene and fuse it to a gene for green fluorescent protein (GFP). Now you can visually observe when the gene is activated. You insert this engineered gene into a host cell and look for GFP expression. You discover some mutants that have different expression levels of GFP and call them GFP1- and GFP2-. The expression levels of GFP are given below. Cell GFP expression Wild type 100 GFP1- 50 GFP2- 0 Propose an explanation for these results based on your model. In other words, what was mutated and how? This answer should include whether the mutation is (view links for more information): dominant or recessive https://www.ncbi.nlm.nih.gov/books/NBK21578/#A1877 in a cis…arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
Human Anatomy & Physiology (11th Edition)BiologyISBN:9780134580999Author:Elaine N. Marieb, Katja N. HoehnPublisher:PEARSON
Biology 2eBiologyISBN:9781947172517Author:Matthew Douglas, Jung Choi, Mary Ann ClarkPublisher:OpenStax
Anatomy & PhysiologyBiologyISBN:9781259398629Author:McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa StouterPublisher:Mcgraw Hill Education,
Molecular Biology of the Cell (Sixth Edition)BiologyISBN:9780815344322Author:Bruce Alberts, Alexander D. Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter WalterPublisher:W. W. Norton & Company
Laboratory Manual For Human Anatomy & PhysiologyBiologyISBN:9781260159363Author:Martin, Terry R., Prentice-craver, CynthiaPublisher:McGraw-Hill Publishing Co.
Inquiry Into Life (16th Edition)BiologyISBN:9781260231700Author:Sylvia S. Mader, Michael WindelspechtPublisher:McGraw Hill Education
Human Anatomy & Physiology (11th Edition)
Biology
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:PEARSON
Biology 2e
Biology
ISBN:9781947172517
Author:Matthew Douglas, Jung Choi, Mary Ann Clark
Publisher:OpenStax
Anatomy & Physiology
Biology
ISBN:9781259398629
Author:McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa Stouter
Publisher:Mcgraw Hill Education,
Molecular Biology of the Cell (Sixth Edition)
Biology
ISBN:9780815344322
Author:Bruce Alberts, Alexander D. Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter Walter
Publisher:W. W. Norton & Company
Laboratory Manual For Human Anatomy & Physiology
Biology
ISBN:9781260159363
Author:Martin, Terry R., Prentice-craver, Cynthia
Publisher:McGraw-Hill Publishing Co.
Inquiry Into Life (16th Edition)
Biology
ISBN:9781260231700
Author:Sylvia S. Mader, Michael Windelspecht
Publisher:McGraw Hill Education
Bacterial Genomics and Metagenomics; Author: Quadram Institute;https://www.youtube.com/watch?v=_6IdVTAFXoU;License: Standard youtube license