PRESCOTT'S MICROBILOGY
11th Edition
ISBN: 9781264075515
Author: WILLEY
Publisher: MCG
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Chapter 17.4, Problem 1MI
What special considerations are necessary if one is constructing a translational fusion of a protein known to be exported?
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Which statement is false:
A) Each type of protein ( ex: hemoglobin vs trypsionngen) varies in the length and amino acid sequence of its peptide
B) After the rpocess of transcription is complete, the mRNA that is produced will continue being tranlsated by ribosomes for the rest of the cells life. mRNA never breaks down
C) A ribosome will bind to an mRNA and will translate the sequence by reading one codon at a time and adding one amino acid to the peptide chain. It will stop the translation once it encounters a stop codon
D) The gene for a protein provides the information on the legth of the peptide, along w the amino acid sequence so the protein can be synthesized by a ribosome
E) Once mRNA has left the nucleus, ribosomes will bind to it and will follow the instructions in its sequence to make the new protien
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.
Define, explain, and differentiate between, the processes of transcription and translation. What enzymes or sub-cellular structures are responsible for carrying out these processes?
Chapter 17 Solutions
PRESCOTT'S MICROBILOGY
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
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- In EUKARYOTIC translation, how does initiation of translation occur? a) What components of the mature mRNA are involved (2 components) and b) what proteins are involved (at least 2 proteins)?arrow_forwardwhat is post-translational protein covalent modification? give three examples and name the enzyme that catalyzes each reaction.arrow_forwardYou are observing the translation process in a eukaryotic cell that has been exposed to an unknown toxin. About halfway through synthesizing the protein, you note that elongation is stalled. Upon closer observation you notice the polypeptide is attached to the tRNA in the A-site, while the P site is occupied by an uncharged tRNA. A possible mechanism that is inhibiting translation is: Question 21 options: eEF-1βγ (beta-gamma) was inhibited from activating eEF-2. Peptidyltransferase activity was inhibited. eEF-2 was inhibited from being activated. eEF-1βγ (beta-gamma) was inhibited from activating eEF-1α (alpha). eEF-1α cannot be released from the aminoacyl-tRNA in the A-site.arrow_forward
- Why nonhomologous end-joining (NHEJ) is helpful ?arrow_forwardWhich among A - D is false regarding antisense RNAS? A) O they occur in protein coding genes B) O they only affect expression of the protein coding genes in which it resides C) O they bind to mRNA D) O they act as translational control mechanism E) Onone are false, A -D are all truearrow_forwardAll translation begin at free ribosomes in the cytosol, yet all secreted proteins are translocated into the ER. What is the one molecule that is responsible for targeting co-translationally translocated proteins to the ER and what are the three events that this molecule mediates between translational initiation and insertion into the ER?arrow_forward
- 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 microsomearrow_forwardProtein X is a soluble, secreted protein. It has an N-terminal ER import sequence that allows it to be translocated into the ER during translation. If you altered the sequence of this protein in the following ways, would it affect its final destination? If yes, explain why and what the new destination would be. If not, explain why. 1) You add an ER retention signal to the protein. 2) You add a nuclear localization signal to the end of the protein sequence.arrow_forwardWhich of the following are elongation factors involved in the attachment of new aminoacyl-tRNAs? EF-Ts EF-Tu EF-p EF-Garrow_forward
- A synthetic mRNA added to a cell-free protein-synthesizing system produces a peptide with the following amino acid sequence: Met-ProIle-Ser-Ala. What would be the effect on translation if the following component were omitted from the cell-free protein-synthesizing system? What, if any, type of protein would be produced? Explain your reasoning. Q. ATParrow_forwardHow does the cell ensure that a specific amino acid (say, valine) attaches itself only to the one tRNA molecule that is specific for valine? (A) Proteins called aminoacyl DNA synthetases are responsible for bringing together the proper pair. The enzymes match the amino acid and one of the correct DNA molecules carrying the right anticodon. (B) Lipids called aminoacyl tRNA synthetases are responsible for bringing together the proper pair. The lipid binds the amino acid and one of the correct tRNA molecules carrying the right codon. (C) Enzymes called aminoacyl tRNA synthetases are responsible for bringing together the proper pair. The enzymes match the amino acid and one of the correct tRNA molecules carrying the right anticodon. (D) Enzymes called peptidyl mRNA synthetases are responsible for bringing together the proper pair. The enzymes match the amino acid and one of the correct mRNA molecules carrying the right anticodon.arrow_forwardWhich of the following mutations in the protein-coding region of a gene is more likely to lead to complete loss of function of the encoded protein: an insertion of six nucleotides or a deletion of two nucleotides? Briefly explain your answer.arrow_forward
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