Prescott's Microbiology
10th Edition
ISBN: 9781259281594
Author: Joanne Willey, Linda Sherwood Adjunt Professor Lecturer, Christopher J. Woolverton Professor
Publisher: McGraw-Hill Education
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Chapter 13, Problem 4CHI
Summary Introduction
The bacterial ribosomes get inactivated when the bacteria enter the
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Place the following steps of the bacterial protein synthesis in their correct order?
Peptide bond formation at the peptidyl-transferase center.
Binding of MRNA and initiator formyl-methionyl-IRNAMet to the 30S ribosomal subunit,
Aminoacylation and formylation of the initiator tRNAMet
Joining of the 30S and the 50S ribosomal subunits,
Release Factor (RF) dependent hydrolysis of the peptidyl RNA and release of the fully synthesized polypeptide from the ribosome.
Elongation Factor G (EF G) dependent translocation of the ribosome by one codon along the MRNA
Elongation Factor Tu (EF-Tu) dependent delivery of an aminoacyl-IRNA to the ribosomal A site
For any antibiotic compounds that don’t appear to inhibit translation of proteins from the ribosome, purpose another potential mechanism whereby this class of antibiotic might be able to act (outside of cell wall/membrane formation). Explain in deatil.
Part A
Shown above is a schematic diagram of the E. coli leader peptidase (Lep) which has several basic amino acids in a cytoplasmic loop. Propose a mutant of Lep that
would be a test of the "inside positive" rule for the orientation of proteins in membranes.
Match the words in the left column to the appropriate blanks in the sentences on the right. Make certain each sentence is complete before submitting
your answer.
terminal
reversed
same
(+)
(-)
center
1. Make mutant Lep that substitutes noncharged residues for the
chains in the loop, and put
charged side chains in
2. If the inside-positive rule applies, the mutant ought to have the
membrane.
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charged side
positions.
orientation in the
Chapter 13 Solutions
Prescott's Microbiology
Ch. 13.1 - MICRO INQUIRY Based on what we now know about...Ch. 13.1 - Retrieve, Infer, Apply 1. Briefly summarize the...Ch. 13.1 - Retrieve, Infer, Apply 2. Explain how protein was...Ch. 13.2 - MICRO INQUIRY To which carbon of ribose...Ch. 13.2 - MICRO INQUIRY How many H bonds are there between...Ch. 13.2 - Prob. 3MICh. 13.2 - Prob. 1RIACh. 13.2 - Retrieve, Infer, Apply What does it mean to say...Ch. 13.2 - Retrieve, Infer, Apply Amino acids are described...Ch. 13.3 - MICRO INQUIRY What provides the energy to fuel...
Ch. 13.3 - MICRO INQUIRY What is the difference between...Ch. 13.3 - MICRO INQUIRY Why cant DNA polymerase I perform...Ch. 13.3 - Retrieve, Infer, Apply How many replicons do...Ch. 13.3 - Retrieve, Infer, Apply Describe the nature and...Ch. 13.3 - Retrieve, Infer, Apply Outline the steps Involved...Ch. 13.3 - Retrieve, Infer, Apply What is the end replication...Ch. 13.4 - Why is the nontemplate strand called the sense...Ch. 13.4 - Retrieve, Infer, Apply The coding region of a gene...Ch. 13.4 - Which strand of a gene has sequences that...Ch. 13.4 - Briefly discuss the general organization of tRNA...Ch. 13.5 - MICRO INQUIRY Are the -35 and -10 regions...Ch. 13.5 - Retrieve, Infer, Apply Outline the transcription...Ch. 13.5 - Retrieve, Infer, Apply What is a polycistronic...Ch. 13.5 - Retrieve, Infer, Apply What is a consensus...Ch. 13.5 - Tabulate the similarities and differences between...Ch. 13.6 - Prob. 1MICh. 13.6 - Retrieve, Infer, Apply List the punctuation codons...Ch. 13.6 - What is the difference between a codon and an...Ch. 13.6 - Retrieve, Infer, Apply What is meant by code...Ch. 13.6 - Retrieve, Infer, Apply Is the genetic code truly...Ch. 13.7 - MICRO INQUIRY Why is simultaneous transcription...Ch. 13.7 - MICRO INQUIRY What would be the outcome if an...Ch. 13.7 - MICRO INQUIRY Why would it be impossible for...Ch. 13.7 - MICRO INQUIRY What provides the energy to fuel...Ch. 13.7 - Retrieve, Infer, Apply In which direction are...Ch. 13.7 - Retrieve, Infer, Apply Briefly describe the...Ch. 13.7 - Retrieve, Infer, Apply What are the translational...Ch. 13.7 - Retrieve, Infer, Apply Tabulate the nature and...Ch. 13.7 - Retrieve, Infer, Apply How many ATP and GTP...Ch. 13.8 - MICRO INQUIRY What are two distinguishing features...Ch. 13.8 - Retrieve, Infer, Apply What are molecular...Ch. 13.8 - Retrieve, Infer, Apply Would an intein-containing...Ch. 13.8 - Retrieve, Infer, Apply Give the major...Ch. 13.8 - Retrieve, Infer, Apply Which translocation or...Ch. 13.8 - Prob. 5RIACh. 13 - Streptomyces coelicolor has a linear chromosome....Ch. 13 - You have isolated several E. coli mutants: Mutant...Ch. 13 - DNA polymerase I (Pol I) of E. coli consists of...Ch. 13 - Prob. 4CHI
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- Antibiotic X binds to the 50S ribosomal subunit of 70S ribosomes and blocks normal ribosomal function. Which of the following is true of this drug? It would interfere with protein synthesis in bacteria, but not affect eukaryotic ribosomes. It would interfere with peptidoglycan syntheis/repair in bacteria, but not affect eukaryotes as they lack peptidoglycan. It would interfere with mRNA transcription in bacteria and in eukaryotes. It would interfere with protein synthesis in bacteria and eukaryotes. It would interfere with mRNA transcription in bacteria, but not affect eukaryotic transcription. It would interfere with peptidoglycan syntheis/repair in bacteria, as well as in eukaryotes that possess cell walls.arrow_forwardRibosomes in the cytoplasm capture mRNA that can be translated into an enzyme for the lysosome. a) Explain what happens from the time the enzyme begins to form in the cytoplasm until it ends up in the lysosome and also explains how the enzyme is transported to the lysosome?arrow_forward1)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 normallyarrow_forward
- You are studying a cytoskeletal accessory protein, AB2. You believe it is involved in receptor-mediated endocytosis allowing for the entry of a novel virus, SARS-CoV X, into the host cell. To confirm that AB2 is required for viral entry, you engineer an AB2 protein containing an N-terminal hydrophobic signal sequence and a C-terminal KDEL sequence (AB2-SSKDEL) and express it in human epithelial airway cells. You compare cells expressing wild-type (WT) AB2 (lacking the signal sequence and KDEL sequence) with cells expressing AB2-SSKDEL. You are looking at the entry of a GFP (green) virus into cells. If AB2 is required for viral entry, via receptor-mediated endocytosis, what results would you expect to see in terms of viral entry? A. WT AB2 - Green ER AB2-SSKDEL - No green ER B. WT AB2-NO green cells AB2-SSKDEL - Many green cells OC. WT AB2 - Many green cells AB2-SSKDEL - NO green cells D.WT AB2 - Green nuclei AB2-SSKDEL - No green nucleiarrow_forwardA 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)?arrow_forwardHow many ribosomes are actively synthesizing proteins at any instant in an E. coli cell growing with a 45-min doubling time? The birth size of E. coli is 1-μm diameter and 2-μm length. The water content is 75%. About 60% of the dry material is protein, and the rate of amino acid addition per ribosome is 20 amino acids per second. The average molecular weight of free amino acids in E. coli is 126.arrow_forward
- Identify the following by describing their functions: EF-G, EF-Tu, EF-Ts, EF-P, and peptidyl transferasearrow_forwardIn the early days of ribosome research, before the exact role of ribosomes was clear, a researcher made the following observation. She could find, in sedimentation experiments on bacterial lysates, not only 3OS, 50S, and 70S particles, but also some particles that sedimented at about 100S and 130S. When she treated such a mixture with EDTA, everything dissociated to 30S and 50S particles. Upon adding divalent ions, she could regain 70S particles, but never 100S or 130S particles. (a) Suggest what the 10oS and 130S particles might represent, in light of cur- rent knowledge of protein synthesis. What important discovery did the researcher miss? (b) Why do you think reassociation to 100S and 130S particles did not work?arrow_forwardAs 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?arrow_forward
- 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.arrow_forwardTetracycline antibiotics bind to the A site on the bacterial ribosome and prevent further translation. Where would you expect polypeptides to accumulate on tetracycline-inhibited ribosomes? Given what tetracycline does, how does this effect cause the bacterial cell to die?arrow_forwardWhat is the major differences between bacteria that use anaerobic vs aerobic respiration and the difference between the 2 processes? Common feautures in the genomic sequences that control transcription between prokaryotes and eukaryotes? Describe some processes of active transport across membranes e g facilitated exocytosis endocytosis active transport?arrow_forward
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