Chapter 13 Translation Flashcards

(43 cards)

1
Q
1) A bacterium's large subunit is 60S and its small subunit is 40S. What is the size of the ribosome containing both subunits?
 A) 20S 
B) 100S 
C) 70S 
D) 120S 
E) 80S
A

E

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2
Q

2) Which of the following is true regarding the tRNA structure?
A) The tRNA binds to an mRNA’s codon at the variable loop.
B) An amino acid binds to the 5′ end of the tRNA molecule.
C) A tRNA molecule that has an amino acid attached to it is called a charged tRNA.
D) The nucleotides found in a tRNA molecule can only be adenine, uracil, guanine, and cytosine.
E) The anticodon is found at the 3′ end of the tRNA molecule.

A

C

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3
Q
3) If humans had 25 amino acids instead of 20 amino acids then how many aminoacyl tRNA synthetases would humans have?
A) 4 
B) 25 
C) 75 
D) 20 
E) 3
A

B

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4
Q

4) During initiation in bacterial translation, a particular mutation causes the premature binding of the large ribosome subunit to the small ribosome subunit. Which component of initiation is not
working properly?

A) IF3
B) Shine-Dalgarno sequence on the mRNA 
C) Ribosome's E site
D) IF2 
E) IF1
A

A

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5
Q

5) A mutation in EF-Tu would have a DIRECT effect on which part of translation?

A) The peptide bond formation would be blocked.
B) The polypeptide would form, but translation termination would be blocked.
C) The small and large subunits would not bind.
D) Translocation would be directly blocked.
E) The next tRNA would not be able to enter the A site of the ribosome.

A

E

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6
Q

6) What signals termination of translation in bacteria?
A) EF-Tu and EF-G
B) a tRNA specific to the stop codon enters the ribosome’s A site
C) ribozymes
D) the stop amino acid is attached to the growing peptide chain
E) RF1 and RF2

A

E

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7
Q
7) A protein is 300 amino acids long. Which of the following could be the number of total nucleotides in the section of DNA that codes for this protein? (Remember: DNA is double-stranded.)
A) 3 
B) 900 
C) 300
D) 100 
E) 1800
A

E

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8
Q

8) The term peptidyl transferase relates to ________.

A) discontinuous strand replication
B) elongation factors binding to the large ribosomal subunit
C) 5′ capping of mRNA
D) peptide bond formation during protein synthesis
E) base additions during mRNA synthesis

A

D

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9
Q

9) X-ray crystallography has revealed and confirmed many details about the ribosome. All of the following are such details, EXCEPT ________.
A) rRNA in the ribosome is in direct contact with the different loops of the tRNA molecule
B) rRNAs are more likely than proteins to be the catalytic molecule of the ribosome
C) the wobble hypothesis is further supported
D) the ribosome is a dynamic structure that changes during its different functional states
E) the distance the tRNA must travel between the E, P, and A sites is considered to be relatively
short

A

E

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10
Q

10) Translation in bacterial and eukaryotic cells has many similarities, but there are also several key differences. Which of the following is one of those differences that is seen in eukaryotes?
A) Eukaryotic ribosomes are smaller with fewer proteins and RNA molecules.
B) Translation and transcription are coupled.
C) Eukaryotes only require one release factor that recognizes all three stop codons.
D) Eukartyotic mRNA contains a Shine—Dalgarno sequence that increases the efficiency of translation.
E) Eukaryotes use the 5′ G-cap and Poly-A-tail on their mRNAs to initiate translation.

A

E

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11
Q
11) The one-gene:one-enzyme hypothesis emerged from work on which two organisms? 
A) Drosophila and humans
B) Neurospora and Drosophila
C) E. coli and yeast
D) E. coli and humans
E) All of the answers listed are correct
A

B

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12
Q

12) By their experimentation using the Neurospora fungus, Beadle and Tatum were able to propose the far-reaching hypothesis that ________.
A) genetic recombination occurred in Neurospora
B) the role of a specific gene is to produce a specific enzyme
C) more than one codon can specify a given amino acid
D) several different enzymes may be involved in the same step in a biochemical pathway
E) prototrophs will grow only if provided with nutritional supplements

A

B

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13
Q

13) A researcher is studying the synthesis of a specific amino acid found in Neurospora. She knows that the pathway begins with a precursor that is converted into the amino acid with two known
intermediates (Substance Blue and Substance Green). She accurately predicts that this amino acid synthesis pathway is catalyzed by three enzymes, (I, II, and III). She subsequently identifies three mutants that she calls Mutant I, Mutant II, and Mutant III. With the information about the mutants below place the enzymes in the order that the enzymes act in this pathway. (Note: the numbers I, II, and III don’t necessarily indicate the order in which the enzymes appear.)
Mutant I (only Enzyme I is mutated) is unable to synthesize the amino acid even if she provided the mutant with both Substance Blue and Substance Green.
Mutant II (only Enzyme II is mutated) is able to synthesize the amino acid if she provided the mutant with Substance Blue or Substance Green.
Mutant III (only Enzyme III is mutated) is able to make the amino acid if she provided the mutant with Substance Green, but not if she provided the mutant with only Substance Blue.
A) I, II, III
B) II, III, I
C) II, I, III
D) III, I, II
E) III, II, I
F) More than one codon can specify a given amino acid.

A

B

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14
Q

14) The β chain of adult hemoglobin is composed of 146 amino acids of a known sequence. In comparing the normal β chain with the β chain in sickle-cell hemoglobin, what alteration is one likely to find?
A) valine instead of glutamic acid in the sixth position
B) glutamic acid replacing valine in the first position
C) frameshift substitutions
D) trinucleotide repeats
E) extensive amino acid substitutions

A

A

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15
Q

15) Often point mutations can cause a protein to be made that differs in just one amino acid. Which of the following changes is most likely to cause the greatest change in protein function?
A) a mutation that replaces a serine with a cysteine
B) a mutation that replaces a valine with an isoleucine
C) a mutation that replaces a glutamic acid with an aspartic acid
D) a mutation that replaces an asparagine with a glutamine E) a mutation that replaces a proline with an aspartic acid

A

E

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16
Q

16) The primary structure of a protein is determined by ________.
A) the sequence of amino acids
B) hydrogen bonds formed between the components of the peptide linkage C) pleated sheets
D) a series of helical domains
E) covalent bonds formed between fibroin residues

A

A

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17
Q

17) The protein shown below provides an example of which level of protein folding?

A) tertiary
B) quaternary 
C) primary
D) pentenary 
E) secondary
A

B

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18
Q
18) Side groups of amino acids are typically classified under which of the following? 
A) primary, secondary
B) linear, circular 
C) alpha, omega 
D) polar, nonpolar
E) long, short
19
Q

19) All of the following are examples of posttranslational modifications, EXCEPT________.

A) Polypeptide chains can be cleaved to produce a shorter and functional polypeptide.
B) The N-terminal amino acid is often removed or modified.
C) Individual amino acid residues are sometimes modified, such as adding a phosphates, acetyl,
or methyl groups can be added.
D) Polypeptides can be degraded and then reassembled to produce entirely different sequenced
polypeptides.
E) Prosthetic groups, such as metals or vitamins, can be added.

20
Q
20) What is the name of the protein that helps fold other proteins into their final and functional form?
A) flippase
B) chaperone 
C) proteasomes 
D) ubiquitin
E) collagen
21
Q
21) Creutzfeldt-Jakob, Huntington, Alzheimer, and Parkinson disease are all characterized with which part of protein synthesis?
A) initiation
B) N-terminal modification 
C) termination
D) elongation
E) protein folding
22
Q
22) Which protein class directly controls many of the metabolic reactions within a cell?
A) operator proteins
B) hydrophilic proteins
C) structural proteins 
D) enzymes
E) repressor proteins
23
Q
23) Modular portions of a protein that fold into stable conformations with specific functional capabilities are referred to as \_\_\_\_\_\_\_\_.
A) protein subunits
B) protein chaperones
C) protein quaternary structures
D) protein secondary structures 
E) protein domains
24
Q

24) Describe the structure of a tRNA molecule. Your answer should include a list of five important sites on the tRNA and two reasons why tRNA’s modified bases are important.

A

The five sites are amino acid binding site, ΤψC stem, variable loop, anticodon stem, D stem, and acceptor stem. The modified bases are important in conferring structural stability and play a role in hydroben bonding between tRNA and
mRNA, which helps explain the wobble effect.

25
25. Assume that a base addition occurs early in the coding region of a gene. Is the protein product of this gene expected to have MORE or FEWER altered amino acids compared with the original gene with a base deletion late in the coding region? Explain.
Since an addition or deletion of a base pair would change every codon after the addition or deletion, then adding a base early in the coding region would change more amino acids than deleting a base later in the coding region.t
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26) The accompanying drawing represents simultaneous transcription and translation in E. coli. The direction of the RNA polymerase is given by the arrow. Picture (a) Is the letter A nearer the 5′ or the 3′ end of the molecule? (b) Is the letter B nearer the 5′ or the 3′ end of the molecule? (c) Is the letter C nearer the 5′ or the 3′ end of the tRNA molecule? (d) What is the "S" value for the large rRNA that is closest to the letter D? (e) Which terminus (N or C) of the growing polypeptide chain is nearer to the letter E?
(a) 3′, (b) 5′, (c) 3′, (d) 23S, (e) N
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27) Consider the roles of IF1, IF2, and IF3 during translation. Predict what the effect would be if IF1, IF2, and IF3 were mutated.
If IF1 was mutated then the second tRNA would bind prematurely to the A site. If IF2 was mutated then the fMET tRNA would not be transferred to the P site of the small ribosome subunit. If IF3 was mutated then the large ribosomal subunit would prematurely bind to the small subunit.
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28) Three major types of RNAs are mRNA, rRNA, and tRNA. For each of the conditions below, predict the consequences in terms of the population of proteins being synthesized in a particular cell and the effects on individual proteins. (a) An acridine dye—induced mutation (adds or deletes single bases in DNA) leads to an mRNA for one protein-producing gene. The condition is heterozygous in the involved cell. (b) A deletion (homozygous) that removes approximately half of the rRNA genes.
(a) Population of proteins: Half of the protein products of that gene will be defective, and the other half will be normal. Individual protein: The protein should show multiple amino acid substitutions "downstream" from the point of the mutation. If a nonsense triplet is introduced, the protein will be shortened in the substituted region. (b) Population of proteins: There would be an overall reduction in protein synthesis. Individual proteins: All of the proteins would be made in their normal form but at reduced levels.
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29) What are polyribosomes and why are they important?
Polyribosomes are clusters of ribosomes held together on an mRNA molecule. This allows for multiple proteins to be synthesized from a single mRNA before it is degraded. This is particularly important in bacteria since they don't protect their mRNA.
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30.Provide five reasons why translation is more complex in eukaryotes compared to bacteria.
There are several possible answers, but could include the following reasons. (1) In eukaryotes, mRNA needs to be transported out of the nucleus prior to it being translated. (2) Eukaryotic ribosomes are larger and are composed of more proteins and rRNA molecules. (3) Translation initiation in bacteria requires the mRNA contain the Shine —Dalgarno sequence. However, in eukaryotes, a more complex initiation process is needed that requires the 5'-G cap and the 3'-poly-A tail. (4) Translation initiation in eukaryotes requires many more initiation factors. (5) There are two tRNAs for methionine in eukaryotes: one for the initiating AUG codon and a different one used for all other AUG codons. (6) Termination in eukaryotes uses one of three possible Release Factors (one for each stop codon) while bacteria have a total of two release factors.
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31) Explain why a eukaryotic mRNA that has begun to be degraded from the 3' end, but still has its complete coding region intact is not efficiently translated.
Eukaryotic translation uses a closed-loop process where the 5' G cap and the 3' poly A-tail of the mRNA loop around and interact with the ribosome to initiate translation. If the 3' poly-A tail has begun to degrade then translation will not efficiently be initiated.
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35) Much has been learned about the relationship between genes and gene products through 35) the use of the mold Neurospora. What specific attributes make Neurospora a good organism for such studies?
Knowledge of its biochemistry; its haploid ascospores; relative ease of isolating nutritional mutations
33
36) Nutritional mutants in Neurospora can be "cured" by treating the medium with substances 36) in the defective metabolic pathway. What determines whether the mutant strain (auxotroph) is "cured" by a particular substance?
The substance needs to be added after the metabolic block in the biochemical pathway.
34
37) Sickle-cell anemia is caused when one nucleotide is changed to another nucleotide in the hemoglobin gene. How does this one small change cause the life-threatening disease of sickle-cell anemia?
Substituting this one nucleotide changes the amino acid from glutamic acid codon to valine. Glutamic acid is a polar negatively charged amino acid whereas valine is a nonpolar. Even though it is only a single base change, the result is a major change in the amino acid that allows the hemoglobin protein to stick to other hemoglobin proteins that results in the sickling of the red blood cell.
35
38) Sickle-cell anemia is caused by a mutation that changes the second nucleotide of the codon from GAG to GUG. This results in a change of the amino acid from glutamic acid to valine. If the mutation affected the third nucleotide of the codon and changed GAG to GAU then the amino acid would change from a glutamic acid to aspartic acid. Would you predict this change to have the same effect?
A change in one polar-charged amino acid to another polar-charged amino acid would be predicted to have less of a phenotype compared to a mutation that resulted in a change from a polar-charged amino acid to a nonpolar amino acid. Changes to the third nucleotide of a codon are often less damaging than changes to the first or second nucleotide.
36
39) In what ways do the amino acid side chains interact to influence protein function?
Higher-level folding of proteins is dependent on a variety of interactions (ionic, covalent, hydrogen, hydrophobic, hydrophilic, etc.), which determine the functional three-dimensional structure of proteins.
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40) Below are several phenomena relating to protein structure. Clearly describe each phenomenon4, 0) the conditions under which each occurs, and the probable influence each has on protein structure. (a) hydrophobic interactions (b) hydrogen bonds (c) disulfide bridges
(a) Hydrophobic interactions: These are nonpolar side chains of amino acids that tend to associate to form hydrophobic clusters usually away from the protein surface. (b) Hydrogen bonds: Such bonds may occur between the components of the peptide bond, the side chains, or a combination of the two. They are responsible for helical and pleated sheet structures of proteins. (c) Disulfide bridges: Such bonds are formed between two cysteine side chains and, because of their covalent nature, represent relatively strong attractive forces between different (sometimes distant) regions of proteins.
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41. Assuming that an amino acid sequence is 250 amino acids long, how many different molecules, each with a unique sequence, could be formed?
20^250
39
42) Regarding the protein structure, how are β-pleated sheets arranged and stabilized?
Several chains run in parallel or antiparallel fashion stabilized by hydrogen bonds formed between components of the peptide linkage.
40
43) Considering the types of side chains on amino acids and their relationship to protein structure, where are the amino acids with hydrophobic side chains most likely to be located?
Away from the water environment and in the interior portion of the molecule
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44) List at least three posttranslational modifications known to occur as a newly synthesized protein matures.
N-terminal removal or modification of an amino acid, modification of some amino acids, addition of carbohydrate side chains, trimming of polypeptide chains, removal of signal sequences, addition of metals
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45) The diseases bovine spongiform encephalopathy and Creutzfeldt—Jakob disease are caused by what kind of protein? How does this protein cause these diseases?
These diseases are caused by the prion protein. The healthy prion (PrPC) is characterized by the secondary structure of alpha helices whereas the diseased prion (PrPSc) is characterized by the secondary structure of beta sheets.
43
46) Which class of protein functions primarily by lowering the energy of activation during a reaction?
Enzyme