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Antibiotics and Protein Synthesis
Antibiotics are molecules produced by microorganisms as defense mechanisms. The most effective antibiotics work by interfering with essential biochemical or reproductive processes. Many antibiotics block or disrupt one or more stages in protein synthesis. Some of these are mentioned here.
Tetracyclines are a family of chemically related compounds used to treat several types of bacterial infections. Tetracyclines interfere with the initiation of translation. The tetracycline molecule attaches to the small ribosomal subunit and prevents binding of the tRNA anticodon during initiation. Both eukaryotic and prokaryotic ribosomes are sensitive to the action of tetracycline, but this antibiotic cannot pass through the plasma membrane of eukaryotic cells. Because tetracycline can enter bacterial cells to inhibit protein synthesis, it will stop bacterial growth, helping the immune system fight the infection.
Streptomycin is used in hospitals to treat serious bacterial infections. It binds to the small ribosomal subunit but does not prevent initiation or elongation; however, it does affect the efficiency of protein synthesis. Binding of streptomycin changes the way mRNA codons interact with the tRNA. As a result, incorrect amino acids are incorporated into the growing polypeptide chain, producing nonfunctional proteins. In addition, streptomycin causes the ribosome to randomly fall off the mRNA, preventing the synthesis of complete proteins.
Puromycin is not used clinically but has played an important role in studying the mechanism of protein synthesis in the research laboratory. The puromycin molecule is the same size and shape as a tRNA/amino acid complex. When puromycin enters the ribosome, it can be incorporated into a growing polypeptide chain, stopping further synthesis because no peptide bond can be formed between puromycin and an amino acid, causing the shortened polypeptide to fall off the ribosome.
Chloramphenicol was one of the first broadspectrum antibiotics introduced. Eukaryotic cells are resistant to its actions, and it was widely used to treat bacterial infections. However, its use is limited to external applications and serious infections. Chloramphenicol destroys cells in the bone marrow, the source of all blood cells. In bacteria, this antibiotic binds to the large ribosomal subunit and inhibits the formation of peptide bonds. Another antibiotic, erythromycin, also binds to the large ribosomal subunit and inhibits the movement of ribosomes along the mRNA.
Almost every step of protein synthesis can be inhibited by one antibiotic or another. Work on designing new synthetic antibiotics to fight infections is based on our knowledge of how the
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Why is targeting protein synthesis an effective strategy for preventing infection?
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Chapter 9 Solutions
Human Heredity: Principles and Issues (MindTap Course List)
- Researchers are studying the mechanism of the antibiotic chloramphenicol. They know that it prevents the formation of peptide bonds during translation. A model of the translation process is shown in the diagram. Which of the following describes where in the model chloramphenicol acts to interfere with the production of proteins from DNA? during initiation during elongation during termination during protein releasearrow_forwardMany antibiotics are effective as drugs to fight off bacterial infections because they inhibit protein synthesis in bacterial cells. Using the information provided in the following table that highlights several antibiotics and their mode of action, discuss which phase of translation is inhibited: initiation, elongation, or termination. What other components of the translational machinery could be targeted to inhibit bacterial protein synthesis? Antibiotic Action 1. Streptomycin Binds to 30S ribosomal subunit 2. Chloramphenicol Inhibits peptidyl transferase of 70S ribosome 3. Tetracycline Inhibits binding of charged tRNA to the A site of the ribosome 4. Erythromycin Binds to free 50S particle and prevents formation of 70S ribosome 5. Kasugamycin Inhibits binding of tRNAfMet 6. Thiostrepton Prevents translocation by inhibiting EF-Garrow_forwardBelow is a picture of a ribosome. Name and give a function of all the “players” of translation found in the picture. Explain what happens during the following steps of translation: Initiation: Elongation: Termination:arrow_forward
- Identify whether each of the following descriptions applies to typical prokaryotic genomes only, typical eukaryotic genomes only, both, or neither, according to lecture. Answer options may be used more than once or not at all. Composed of double-stranded DNA only. Each chromosome has a centromere. Species with larger genomes have more genes. [Choose ] [Choose ] prokaryotes only neither eukaryotes or prokaryotes eukaryotes only both prokaryotes and eukaryotes [Choose ]arrow_forwardA __________ molecule is characterized by having a peptide-binding site, a modified 5’ guanine, and an anticodon. _____________ molecules are encoded by multiple gene copies in both prokaryotes and eukaryotes, and they catalyze critical reactions functions during translation. Group of answer choices mRNA; rRNA rNA; aminoacyl tRNA synthase tRNA; rRNA rRNA; precursor RNA mRNA; tRNAarrow_forwardChoose the effect of the given agents to translation or transcription. CHOICES: prevention of ribosomal movement in eukaryotes our email will be recorded when you submit thi prevention of ribosomal movement in prokaryotes RNA polymerase II inhibition RNA polymerase inhibition disruption of elongation stage of translation Tetracycline * Puromycin * Amanitin * Rifampicin * Diphtheria Toxin *arrow_forward
- Indicate the class of drug that is stopping polypeptide translation: change 30S subunit block ribosome attachment inhibits peptide bonding block ribosome movement block tRNA dockingarrow_forwardWhich of the following is NOT true of deoxyribonucleic acid (DNA)? Stores genetic information that can be expressed within a bacterial cell, transferred "vertically" to offspring cells, or "horizontally" to other recipient cells Serves as a template for the transcription of mRNA Each DNA nucleotide contains the sugar ribose, phosphate, and one of the following nitrogenous bases: adenine, uracil, guanine, or cytosine Found as a circular molecule in bacteria, either as chromosomes or plasmids None of the other four answers (all are true of DNA)arrow_forwardWhich of the following statements about translation is false? In eukaryotes, the 5' cap and the 3' poly(A) tail are involved in translation initiation. Peptidyl-transferase activity during translation is the property of a ribozyme. A base at the first position of an anticodon on the tRNA would pair with a base at the third position of the mRNA. The growing peptide chain is transferred from the tRNA in the P site to the tRNA in the A site. Ribosomes move along an mRNA in the 3’ → 5' direction.arrow_forward
- Rank from left to right the compound with the most reactive chemical linkage: peptide bond, ester, ether, acid anhydride, aminoacyl-TRNA How many bacterial translation factors are "G" proteins? How many proteins are involved in the nucleotide-dependent steps of protein synthesis?arrow_forwardPolypeptides can be reversed back to RNA because of the enzyme transcriptase. The genetic material must be replicated with high fidelity and great speed. Eukaryotic mRNA is said to be polycistronic since they encode multiple polypeptide chains RNA-synthesis occurs inside the nucleus while protein synthesis in the cytoplasm of eukaryotic organisms. Write T if the statement is true and write F if the statement is falsearrow_forwardAn RNA polymer is made by using the enzyme polynucleotide phosphorylase with equal quantities of CTP and GTP. When this RNA is used in an in vitro translation system, all of the following amino acids could be incorporated into a newly made polypeptide, except: glycine (Gly) histidine (His) proline (pro) alanine (Ala) arginine (Arg)arrow_forward
Human Heredity: Principles and Issues (MindTap Co...BiologyISBN:9781305251052Author:Michael CummingsPublisher:Cengage Learning