Chapter 27 Protein MetabolismMultiple Choice Questions 1. The genetic code Page: 1038 Difficulty: 2 Ans: C A certain bacterial mRNA is known to represent only one gene and to contain about 800 nucleotides. If you assume that the average amino acid residue contributes 110 to the peptide molecular weight, the largest polypeptide that this mRNA could code for would have a molecular weight of about: A) B) C) D) E) 800. 5,000. 30,000. 80,000. An upper limit cannot be determined from the data given. 2. The genetic code Page: 1038 Difficulty: 2 Ans: C Assuming that the average amino acid residue contributes 110 to the peptide molecular weight, what will be the minimum length of the mRNA encoding a protein of molecular weight 50,000? A) B) C) D) E) 133 nucleotides 460 nucleotides 1,400 nucleotides 5,000 nucleotides A minimum length cannot be determined from the data given. 3. The genetic code Pages: 1039-1044 Difficulty: 3 Ans: D Which of the following are features of the wobble hypothesis? A) B) C) D) E) A naturally occurring tRNA exists in yeast that can read both arginine and lysine codons. A tRNA can recognize only one codon. Some tRNAs can recognize codons that specify two different amino acids, if both are nonpolar. The “wobble” occurs only in the first base of the anticodon. The third base in a codon always forms a normal Watson-Crick base pair. 4. The genetic code Page: 1039 Difficulty: 2 Ans: C Which one of the following is true about the genetic code? A) B) C) D) All codons recognized by a given tRNA encode different amino acids. It is absolutely identical in all living things. Several different codons may encode the same amino acid. The base in the middle position of the tRNA anticodon sometimes permits “wobble” base pairing with 2 or 3 different codons. E) The first position of the tRNA anticodon is always adenosine. Protein synthesis Page: 1051 Difficulty: 2 Ans: A Aminoacyl-tRNA synthetases (amino acid activating enzymes): A) B) C) D) E) “recognize” specific tRNA molecules and specific amino acids. any given tRNA molecule will accept any of the 20 amino acids. require GTP to activate the amino acid. role. . Protein synthesis Page: 1049 Difficulty: 2 Ans: A Which of the following statements about tRNA molecules is false? A) A.000. There are two major subunits. C. The tRNA must contain the sequence UUU. 9. It will accept only the amino acid phenylalanine. E) There is at least one tRNA for each of the 20 amino acids. 6. and U are the only bases present in the molecule. the small subunit does not. They contain several short regions of double helix. each molecule contains several short. G.000.314 Chapter 27 Protein Metabolism 5. Protein synthesis Page: 1045 Difficulty: 1 Ans: D Which one of the following statements about ribosomes is true? A) B) C) D) E) The large subunit contains rRNA molecules. in conjunction with another enzyme attach the amino acid to the tRNA. There are about 25 of them in an E. occur in multiple forms for each amino acid. with molecular weights less than 10. With the right enzyme. Their anticodons are complementary to the triplet codon in the mRNA. Protein synthesis Page: 1051 Difficulty: 2 Ans: E Which of the following is not true of tRNA molecules? A) B) C) D) E) The 3'-terminal sequence is —CCA. D) The amino acid attachment is always to an A nucleotide at the 3' end of the molecule. interact directly with free ribosomes. B) Although composed of a single strand of RNA. 7. The RNA in ribosomes plays a structural. They contain more than four different bases. not catalytic. They are relatively small. doublehelical regions. coli cell. each with multiple proteins.) A) B) C) D) E) It interacts specificially with the Phe synthetase. Phenylalanine can be specifically attached to an —OH group at the 3' end. Its molecular weight is about 25. C) Any given tRNA will accept only one specific amino acid. 8. Protein synthesis Page: 1050 Difficulty: 2 Ans: E Which of the following statements about the tRNA that normally accepts phenylalanine is false? (mRNA codons for phenylalanine are UUU and UUC. require a tRNA. mRNA. coli. 14. Protein synthesis Page: 1056 Difficulty: 2 Ans: A Formation of the ribosomal initiation complex for bacterial protein synthesis does not require: A) B) C) D) E) EF-Tu. attaches a specific amino acid to any available tRNA species. one to form the aminoacyl adenylate. and GTP as substrates. Protein synthesis Page: 1051 Difficulty: 2 Ans: D In the “activation” of an amino acid for protein synthesis: A) B) C) D) E) leucine can be attached to tRNAPhe. Protein synthesis Page: 1051 Difficulty: 2 Ans: B In E. Protein synthesis Pages: 1051-1054 Difficulty: 2 Ans: D Which of the following statements about aminoacyl-tRNA synthetases is false? A) B) C) D) E) Some of the enzymes have an editing/proofreading capability. Protein synthesis Page: 1051 Difficulty: 2 Ans: D The enzyme that attaches an amino acid to a tRNA (aminoacyl-tRNA synthetase): A) B) C) D) E) always recognizes only one specific tRNA. an amino acid. the amino acid is attached to the 5' end of the tRNA through a phosphodiester bond. The enzyme splits ATP to AMP + PPi. two separate enzymes are required. The enzyme attaches an amino acid to the 3' end of a tRNA. initiation factor 2 (IF-2). The enzyme will use any tRNA species. then attached to a specific tRNA. 13. each of which attaches amino acids to different ends of the tRNA. there is at least one specific activating enzyme and one specific tRNA for each amino acid. are amino acid–specific. 11.Chapter 27 Protein Metabolism 315 10. There is a different synthetase for every amino acid. 12. attaches the amino acid at the 5' end of the tRNA. but is highly specific for a given amino acid. aminoacyl-tRNA synthetases: A) B) C) D) E) activate amino acids in 12 steps. . splits ATP to ADP + Pi. formylmethionyl tRNAfMet. catalyzes formation of an ester bond. fall into two classes. there is at least one enzyme specific for each amino acid. the other to attach the amino acid to the tRNA. by the aminoacyl-tRNA synthetase specific for leucine. methionine is first formylated. have no proofreading activities. GTP. have specific. ribosome. Protein synthesis Page: 1062 Difficulty: 1 Ans: B The large structure consisting of a mRNA molecule being translated by multiple copies of the macromolecular complexes that carry out protein synthesis is called a: A) B) C) D) E) lysosome. Elongation factor EF-Tu facilitates translocation. Protein synthesis Page: 1058 Difficulty: 2 Ans: E Which one of the following statements about the elongation phase of protein synthesis is true? A) B) C) D) At least five high-energy phosphoryl groups are expended for each peptide bond formed. An mRNA is never degraded but is passed on to the daughter cells at cell division. 17. contain at least one catalytic RNA molecule (ribozyme). 18. GTP. ribosomes move along the mRNA in the direction 5' → 3'. Protein synthesis Page: 1059 Difficulty: 2 Ans: C Which of the following statements about bacterial mRNA is true? A) B) C) D) E) A ribosome usually initiates translation near the end of the mRNA that is synthesized last. synthosome. Protein synthesis Page: 1058 Difficulty: 2 Ans: D In bacteria the elongation stage of protein synthesis does not involve: A) B) C) D) E) aminoacyl-tRNAs. require puromycin for normal function. Protein synthesis Page: 1059 Difficulty: 2 Bacterial ribosomes: A) B) C) D) E) Ans: B bind tightly to specific regions of DNA. Peptidyl transferase catalyzes the attack of the carboxyl group of the incoming amino acid on an ester linkage in the nascent polypeptide. E) Peptidyl transferase is a ribozyme. Ribosomes cannot initiate internally in a polycistronic transcript. . polysome. During elongation. contain three species of RNA and five different proteins. proteosome. During polypeptide synthesis. EF-Tu. The codon signaling peptide termination is located in the mRNA near its 5' end.316 Chapter 27 Protein Metabolism 15. different binding sites for each of the 20 tRNAs. peptidyl transferase. IF-2. 19. 16. forming polysomes. incoming aminoacylated tRNAs are first bound in the P site. Protein targeting and degradation Pages: 1069-1070 Difficulty: 2 Ans: A Glycosylation of proteins inside the endoplasmic reticulum does not involve: A) B) C) D) E) a His residue on the protein. The signal peptide is cleaved off inside the mitochondria by signal peptidase. Protein targeting and degradation Page: 1069 Difficulty: 2 Ans: D Which of the following is true about the sorting pathway for proteins destined for incorporation into lysosomes or the plasma membrane of eukaryotic cells? A) B) C) D) Binding of SRP to the signal peptide and the ribosome temporarily accelerates protein synthesis. dolichol phosphate. N-acetylglucosamine. and (4) mRNA for hemoglobin. where in the newly synthesized hemoglobin would the Ala from Ala-tRNACys be incorporated? A) B) C) D) E) Nowhere. E) The signal sequence is added to the polypeptide in a posttranslational modification reaction. . an Asn residue on the protein. Protein synthesis Pages: 1066-1067 Difficulty: 2 Ans: C Which one of the following antibiotics does not function by interfering with the translational process? A) B) C) D) E) Chloramphenicol Cycloheximide Penicillin Puromycin Streptomycin 22.Chapter 27 Protein Metabolism 317 20. (3) all of the cofactors and enzymes needed to make protein in vitro. The signal recognition particle (SRP) binds to the signal peptide soon after it appears outside the ribosome. this is the equivalent of a nonsense mutation Wherever Ala normally occurs Wherever Cys normally occurs Wherever either Ala or Cys normally occurs Wherever the dipeptide Ala-Cys normally occurs 21. glucose. 23. (2) all the other tRNAs and amino acids. If the resulting Ala-tRNACys were added to a mixture of (1) ribosomes. Protein synthesis Page: 1061 Difficulty: 3 Ans: C It is possible to convert the Cys that is a part of Cys-tRNACys to Ala by a catalytic reduction. The newly synthesized polypeptides include a signal peptide at their carboxyl termini. 1. 2. Leu. 4. 4. 1. Phe. a lysine-containing target sequence in the protein. tunicamycin. Gly. Protein targeting and degradation Page: 1071 Difficulty: 2 Ans: D The signal sequences that direct proteins to the nucleus are: A) B) C) D) E) always at the amino terminus of the targeted protein. SecA pushes 20 amino acids of the polypeptide into the translocation complex. 2. Asp. the amino-terminus of the protein. and many of the signals remain unknown. cycloheximide. which occur in what order for correct export? 1. puromycin. A chaperone.318 Chapter 27 Protein Metabolism 24. A) B) C) D) E) A chaperone. etc. 3 2. 3 2. 4. Lys. etc. SecA. 4 1. 26. SecB. 2 27. 3. the carboxy-terminus of the protein. Met. streptomycin. glycosyl moieties containing mannose 6-phosphate residues. binds to the polypeptide. Protein targeting and degradation Page: 1076 Difficulty: 3 Ans: D Ubiquitin-mediated protein degradation is a complex process. and are located at: A) B) C) D) E) a helix-turn-helix motif in the protein. binds to the polypeptide. 3. . coli includes the following steps. 1. 3. Protein targeting and degradation Page: 1070 Difficulty: 2 Ans: E Posttranslational glycosylation of proteins is inhibited specifically by: A) B) C) D) E) chloramphenicol. One known signal involves recognition of amino acids in a processed protein that are either stabilizing (Ala. 25. 2. the same as those that direct certain proteins to lysosomes.). 4. cleaved after the protein arrives in the nucleus. a zinc finger structure in the protein. Ser. Protein targeting and degradation Pages: 1072-1074 Difficulty: 3 Ans: C The pathway for polypeptides exported from E. not located at the ends of the peptide. but in its interior. 1. 4 3. ATP is hydrolyzed by Sec A.) or destabilizing (Arg. Ans: When one or two nucleotides were added to or deleted from a gene. The genetic code Page: 1036 Difficulty: 3 You have isolated a fragment of viral DNA that totally encodes at least two proteins. again starting from the 5' end and using only the first reading frame? . the resulting mRNA produced a protein with a different amino acid sequence after the deletion or insertion. Because only that aminoacyl-tRNA whose anticodon matched the trinucleotide “mRNA” was bound. if it were. The genetic code Pages: 1035-1036 Difficulty: 2 Outline one of the experimental methods providing evidence that the genetic code was a triplet code. the coding specificity of each sequence of three bases could be determined by determining which of the 20 aminoacyl-tRNAs bound.Chapter 27 Protein Metabolism 319 Short Answer Questions 28. The identities and ratios of the amino acids specified by such polymers provided important clues that helped solve the genetic code.) (c) Suppose the other (complementary) strand is used as a template for transcription. showing that UUU encodes Phe. p. (a) Why might you consider this unusual? (b) You sequence the two proteins and find no sequence homology. One possible explanation is that the two genes coding for these proteins overlap and are read in different reading frames. there would be 80 amino acid residues of identical sequence in the two proteins. 120 and 80 amino acids long. For example. succinctly. 1038. poly(U) (containing only the codon UUU) directed the synthesis of polyphenylalanine. the resulting protein had a normal sequence except for the insertion or deletion of a single amino acid residue. three..g. 30. or four base pair sequences. The genetic code Page: 1036 Difficulty: 3 Describe. only one of the 20 amino acids was converted into protein. Ans: (1) When synthetic polymers of only one nucleotide were used as mRNA in vitro. What is the amino acid sequence of the resulting peptide. 70% A and 30% T) generate only certain codons in predictable ratios. (3) Random polymers of RNA containing known ratios of nucleotides (e. The DNA fragment is 400 base pairs long. two ways in which synthetic polynucleotides were used in solving the genetic code (you need not describe how the synthetic polynucleotides were made). 31. 27-7. Ans: (a) Two distinct proteins of these sizes should require mRNAs of 360 and 240 base pairs because each amino acid residue requires 3 base pairs to code for it. (4) Additional assignments were made possible using synthetic oligonucleotides containing repeats of specific two. Propose a model to account for these findings. The genetic code Page: 1038 Difficulty: 2 The template strand of a segment of double-stranded DNA contains the sequence: (5')CTT TGA TAA GGA TAG CCC TTC (a) What is the base sequence of the mRNA that can be transcribed from this strand? (b) What amino acid sequence could be coded by the mRNA base sequence in (a). (2) Trinucleotides of known sequence were used to stimulate aminoacyl-tRNA binding to ribosomes. 29. (b) No homology means that the smaller protein cannot be derived from the larger by proteolysis. When three nucleotides were added or deleted. using only the first reading frame starting at the 5' end? (Refer to Fig. The genetic code Page: 1038 Difficulty: 3 Describe the possible outcomes that could occur because of a single base change in an mRNA Ans: The most likely result is a single amino acid change in the encoded protein. The genetic code Pages: 1039-1044 Difficulty: 2 In protein synthesis. 1038. when a codon is altered to one of another amino acid. 1038. Their corresponding amino acid sequences are: Mutant 1 2 3 4 5 MET-Ser-Ile-Arg Leu-TRP-Ile-Arg Leu-Ser-ARG-Arg Leu-Ser-Ile-PRO Leu-Ser-Ile-TRP What was the nucleotide sequence of the region of mRNA that coded for the amino acid sequence in the wild-type organism? (Refer to Fig. Several mutants were isolated. No peptide would be produced because of the stop codons. Why then does the cell require only 32 different tRNAs to recognize 61 different codons? Ans: Certain tRNAs have the unusual nucleotide inosinate in the first anticodon position.) 32. while alteration of the normal stop codon to a “sense” codon will result in a lengthened protein. p. if the altered codon still specifies the original amino acid. and result in no protein product. “wobble” in the third base pair allows one tRNA to read three different codons. However. 27-6. The genetic code Page: 1038 Difficulty: 3 The following sequence of four amino acids occurred in the structure of a polypeptide found in a wild-type organism: Leu-Ser-Ile-Arg.320 Chapter 27 Protein Metabolism Ans: (a) (5')GAA GGG CUA UCC UUA UCA AAG(3’) (b) Glu-Gly-Leu-Ser-Leu-Ser-Lys (c) The codons translate to Leu-Stop-Stop. Because inosinate can base pair with A. there is a standard anticodon-codon base pair with the first two bases of the codon. Base pairing between the codon and the tRNA anticodon assures that the correct amino acid will be inserted into the nascent polypeptide chain. or mRNA turnover rates. In each recognized codon. Changes in mRNA sequence outside the protein-coding region may affect translational efficiency. U. (See also Fig. 27-6. tRNAs with U or G in the first anticodon position also exhibit a wobble effect that permits pairing with two different codons. 61 codons specify the 20 amino acids. 33. splicing. . each of which carried a single base pair change in the region of DNA that coded for this amino acid sequence. p. a tRNA containing hypoxanthine can recognize three different codons. Conversion to a nonsense codon will result in a truncated polypeptide. some nucleotide changes will be “silent” and not change the protein. or C. Similarly. Alternation of the initiaton codon may result in the total failure to translate.) Ans: (5')C or (5')U UG UCG AUA CGG 34. 37. Ans: There are two main stages of selection: 1) the synthetase strongly favors activation of the correct amino acid to become aminoacyl-AMP (incorrect amino acids are very poorly activated) and 2) when the correct uncharged tRNA is bound to the enzyme.Chapter 27 Protein Metabolism 321 35. only completed polypeptides were isolated and analyzed for the amount of redioactivity in different regions. Protein synthesis Pages: 1053-1054 Difficulty: 2 The recognition of an amino acid by its cognate aminoacyl-tRNA synthetase is said to involve a “second genetic code”. large ribosomal subunits. are rapidly hydrolyzed). The “second code” refers to features common to all tRNAs that carry the same amino acid. The opposite is true for the termination point. 1053. or require ten or more specific nucleotides throughout the sequence. Protein synthesis Pages: 1051-1053 Difficulty: 2 The process of charging tRNAs with their cognate amino acids involves multiple proofreading steps to increase the overall fidelity. The greatest radioactivity should be located in the region furthest from the initiation point and the least radioactivity in the region closest to the initiation point. Describe the analysis and how it demonstrated the direction of chain growth. T. F 36. Protein synthesis Page: 1055 Difficulty: 3 In 1961. These features occur at different places in different tRNA classes. The experiment involved the analysis of hemoglobin molecules that were being synthesized in reticulocytes in the presence of radioactive amino acids. ___There are four binding sites for aminoacyl-tRNAs on a ribosome. ___A ribosome is the complex within which protein synthesis occurs. p. In addition. 27-16. F. The analysis showed that polypeptide synthesis was initiated at the amino terminus and terminated at the carboxyl terminus. (See Fig. though they may become bound. if their tRNA does manage to become acylated by the wrong amino acid. Ans: T. Briefly describe these steps. ___Ribosomes contain many separate proteins. only the correct aminoacyl-AMP is tolerated in the “proofreading” active site (incorrect aminoacyl-AMPs. and may be as simple as a single G-U basepair. that product is also rapidly hydrolyzed. Ans: In the experiment. Protein synthesis Pages: 1045-1049 Difficulty: 1 Indicate whether the following statements are true (T) or false (F). for most synthetases. . but many have multiple cognate tRNAs that must be charged (aminoacylated). making them specifically recognizable by the correct synthetase.) 38. Howard Dintzis carried out an experiment that defined the direction of polypeptide chain growth during protein synthesis in cells. ___The three ribosomal RNAs in a bacterial ribosome are distributed in three separate. What is meant by this? Ans: Each of the 20 amino acids has a unique synthetase. d. Protein synthesis Pages: 1056-1061 Difficulty: 2 Indicate whether each of the following statements is true (T) or false (F). but no NTP hydrolysis. ___Aminoacyl-tRNA binding to the A site of the ribosome requires the accessory factor EF-G and GTP hydrolysis. 40. T. (a) Initiation factor 2 (IF-2) (b) 16S RNA (c) Peptidyl transferase (d) Release factors (e) Elongation factor G (EF-G) (f) N10-formyltetrahydrofolate (g) ATP (h) tRNAfMet . the Shine-Dalgarno sequence in the mRNA base pairs with a complementary sequence in the 16S RNA of the ribosome. the initiating AUG codon is the first AUG that the ribosome encounters as it scans the mRNA from its 5' end. In eukaryotes.322 Chapter 27 Protein Metabolism 39. ___Termination of translation requires release factors. T 42. F. In both cases the initiating AUG also sets the correct reading frame. Protein synthesis Pages: 1056-1061 Difficulty: 1 Match the factor or enzyme at the right with the stage(s) of protein synthesis at which it acts. indicate both of them. Describe how prokaryotes and eukaryotes determine the correct reading frame. ___Aminoacylation or “charging” of tRNA requires the formation of an aminoacyl-AMP intermediate. Ans: In prokaryotes. If a factor or enzyme participates in two stages of protein synthesis. b. Protein synthesis Page: 1056-1058 Difficulty: 3 A given mRNA sequence might be translated in any of three reading frames. ___ ___ ___ ___ Amino acid activation Initiation Elongation Termination (a) RF1 (b) EF-Tu (c) aminoacyl-tRNA (d) Shine-Dalgarno sequence Ans: c. a 41. ___Assembly of a complete ribosome onto an mRNA requires ATP hydrolysis. Protein synthesis Pages: 1056-1061 Difficulty: 3 Briefly describe the role of the following components in bacterial protein synthesis. Thus. this positions the correct start codon (AUG) on the 30S ribosomal subunit. T. the initiating AUG is distinguished by its proximity to the Shine-Dalgarno sequence. Ans: F. ___Translocation of a growing polypeptide from the A to the P site on the ribosome requires EFG and GTP hydrolysis. brings the fMet-tRNAfMet to the initiation complex. which donates the aminoacyl group to tRNA. F. 1 44. T 45. indicate whether each of the following statements is true (T) or false (F). ___ Aminoacyl-tRNA binds to the A site. ___ In prokaryotes it is initiated with Met whereas in eukaryotes it is initiated with fMet. and helps to line up the mRNA initiation AUG codon on the ribosome. ___ Bacterial mRNA consists only of the bases that code for amino acids. T . coli. (f) N10-formyltetrahydrofolate is the cofactor that donates a methyl group in the conversion of tRNA-bound Met to fMet. ___ Polysomes do not necessarily contain mRNA. Protein synthesis Pages: 1057-1058 Difficulty: 2 Ans: B Regarding translation in eukaryotes versus that in prokaryotes (bacteria). ___ Peptide bond formation shifts the growing peptide from the P to the A site. ___ In eukaryotes the 3' end of the mRNA is associated with the 5' end during initiation whereas in prokaryotes it is not. Ans: T. Ans: T. ___ The 50S subunit binds to the initiation complex of the 30S subunit and mRNA. ___ Bacterial mRNA is broken down within a few minutes of its formation in E. It catalyzes formation of each peptide bond as the ribosome moves along the mRNA. F. ___ In prokaryotes it is initiated at an AUG near a Shine-Dalgarno sequence in the mRNA whereas in eukaryotes it is initiated at an AUG near the 3' end of the mRNA. 4. (e) EF-G participates in the translocation of the ribosome down the mRNA by one codon after each peptide bond is formed. Ans: 2. 43.Chapter 27 Protein Metabolism 323 Ans: (a) IF-2 is a protein factor that. ___ Bacterial mRNA can be translated while it is still being synthesized. F. the other containing anticodons. (d) Release factors are proteins that bring about the release of the finished polypeptide when the ribosome encounters a termination codon in the mRNA. ___ Bacterial mRNA normally occurs as a double-stranded structure. (b) 16S RNA is a component of the small (30S) subunit. F. (h) tRNAfMet is the transfer RNA that initiates protein synthesis by inserting the first amino acid (fMet) in every prokaryotic protein. it donates an AMP residue in the formation of aminoacyl adenylate. Protein synthesis Pages: 1056-1062 Difficulty: 2 Indicate whether each of the following statements is true (T) or false (F). F. (c) Peptidyl transferase is a ribozyme in the 50S ribosomal subunit. when bound to GTP. It contains a sequence complementary to the Shine-Dalgarno sequence in the mRNA. with one strand containing codons. Protein synthesis Pages: 1056-1061 Difficulty: 2 Number the following steps in the proper order with regard to protein synthesis. 3. ___ In prokaryotes translation and transcription are coupled whereas in eukaryotes they are not. ___ Deacylated tRNA is released from ribosome. (g) ATP is the substrate for aminoacyl-tRNA synthetases. Protein synthesis Pages: 1062-1065 Difficulty: 2 Following the synthesis of their polypeptide chain. What are these steps and what cellular components are necessary for each of them to occur? Ans: The three steps are: (1) An aminoacyl-tRNA is brought to the A site by EF-Tu with bound GTP. 5) isoprenylation of Cys side-chains. synthosome. This shifts the peptidyl-tRNA to the A site and the deacylated tRNA to the E site. carboxylation. Protein synthesis Pages: 1058-1061 Difficulty: 2 Polypeptide chain elongation in E. (2) peptidyl transferase (a ribozyme) catalyzes peptide-bond formation. This allows the insertion of an amino acid instead of the chain termination that would normally have occurred at the point of a nonsense (stop) codon. etc. coli occurs by the cyclical repetition of three steps. 4) attachment of N-linked (to Asn) or O-linked (to Ser or Thr) oligosaccharide moieties. etc. Protein synthesis Page: 1060 Difficulty: 2 A new antibiotic was recently discovered that inhibits prokaryotic protein synthesis. 50. List and describe briefly at least four possible types of modification that can occur. ribosome. biotin. helped by EF-G (translocase). proteosome. 47. . protein synthesis can be initiated. 48. 49. methylation. 2) removal of signal sequences used for targeting. 7) processing of proenzymes or zymogens. but only dipeptides that remain bound to the ribosome are formed. What specific step of protein synthesis is likely to be blocked by this antibiotic? Ans: The antibiotic probably blocks translocation. which allows it to base pair with one of the stop codons. Ans: 1) Amino-terminal modification (N-acetylation or deacetylation). polysome.). 6) incorporation of prosthetic groups (heme. (3) the ribosome translocates three nucleotides down the mRNA. Protein synthesis Page: 1065 Difficulty: 3 In no more than three sentences. In the presence of the antibiotic. many proteins require further posttranslational modifications before they attain their full biological activity or function.324 Chapter 27 Protein Metabolism 46. Protein synthesis Page: 1062 Difficulty: 1 Ans: B The large structure consisting of a mRNA molecule being translated by multiple copies of the macromolecular complexes that carry out protein synthesis is called a: A) B) C) D) E) lysosome. and 8) formation of disulfide crosslinks. Ans: A suppressor tRNA has one or more altered bases in its anticodon.). 3) side-chain modification (phosphorylation. describe a nonsense suppressor tRNA and how it differs from a normal tRNA. Importin α and β are then exported from the nucleus. NLS-carrying proteins can be reimported to fulfill their function. Protein targeting and degradation Page: 1068-1069 Difficulty: 2 When first synthesized. The presence of ubiquitin targets the protein for degradation by cellular proteases. which is then bound to a nuclear pore. Ran GTPase mediates translocation of this complex into the nucleus. distributing the nuclear contents throughout the cell. ubiquitin is finally joined through its carboxyl terminus to a lysine ε-amino group in the protein to be degraded. (3) The SRP-ribosomenascent chain complex binds to the ribosome and SRP receptors on the cytosolic face of the ER. also yielding a thioester link. from which it enters the Golgi complex and is packaged into a secretory vesicle for secretion by exocytosis. where importin β dissociates from importin α. (5) The signal sequence is cleaved. The carboxyl-terminal residue of ubiquitin is first activated by the formation of a thioester with the first enzyme in the pathway in an ATP-dependent reaction. proinsulin has an additional leader or signal peptide at its amino terminus. with the newly synthesized polypeptide crossing into the ER lumen as it grows. the SRP then dissociates. what is the likely function of the signal peptide? Ans: The leader peptide in proinsulin is a signal sequence directing it to the endoplasmic reticulum. Protein targeting and degradation Page: 1075 Difficulty: 3 Describe the role of ubiquitin in mediating intracellular protein breakdown. . (2) The amino-terminal portion of the nascent chain. 53. When the nuclear envelope is reestablished. is covalently joined to proteins targeted for degradation. This complete molecule is called preproinsulin and the signal peptide is cleaved off to give proinsulin. After displacement of the first enzyme by a second. and importin α releases the nuclear protein. Ans: (1) The mRNA forms an initiation complex with a cytoplasmic ribosome and transcription begins. and why are the targeting sequences not removed upon arrival of the protein in the nucleus? Ans: In the cytoplasm. Ans: Ubiquitin. interrupting polypeptide elongation. Protein targeting and degradation Page: 1069 Difficulty: 2 Describe the sequence of events between the transcription of an mRNA for a secreted protein and the arrival of that protein in the lumen of the endoplasmic reticulum. a protein found in all eukaryotic cells. where eukaryotic protein synthesis occurs.Chapter 27 Protein Metabolism 325 51. (4) Chain elongation continues. The nuclear envelope of higher eukaryotes breaks down at each cell division. binds to an SRP (signal recognition particle). 52. 54. Briefly. containing a signal sequence. Protein targeting and degradation Pages: 1071-1073 Difficulty: 2 What are the stages in targeting of nuclear proteins. and available for another cycle of import. proteins carrying nuclear localization signal (NLS) sequences are bound by a complex of importin α and β.
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