Which functional site is found in the small subunit of the ribosome? peptidyl transferase centre O decoding centre
Q: Place the following steps of the bacterial protein synthesis in their correct order? Peptide bond…
A: Transcription is a process in which one strand of DNA known as template strand is known as converted…
Q: During charging of tRNAs
A: Answer: tRNA : It is known as transfer-Ribonucleic Acid, which is used in translation of mRNA using…
Q: What does the A site on the ribosome do? What does the P site on the ribosome do?…
A: The ribosome is a complex molecule made up of ribosomal RNA molecules and proteins that functions as…
Q: EF-tu binds to the 3'end of charged tRNAs can only bind a charged tRNA when it is…
A:
Q: Which of these is a post-translational modification that targets a protein to the proteasome? LO…
A: Post-translational modifications include changes in the polypeptide chain after its synthesis during…
Q: An aminoacyl-tRNA is initially bound to the ribosome in prokaryote at the A site on the 70S subunit…
A: A small RNA molecule known as transfer RNA (tRNA) is essential for the production of proteins.…
Q: How does tRNA move through the 3 sites of the ribosome (in what order)
A: tRNA or the transfer RNA is the adaptor molecule possessing a clover leaf-shaped structure due to…
Q: Which of these molecules is responsible for bringing the correct amino acid to the ribosome? acetyl…
A: Translation is the process by which the cells of the body prepare their own proteins in the…
Q: Which of the following is responsible for synthesizing MRNA? O DNA O RNA polymerase O TRNA O None of…
A: The central dogma of life comprises of two main processes, transcription and translation process…
Q: Which of the following is the most likely reason that many ribosomes do not attach to the surface of…
A: A ribosome is an intercellular structure composed of RNA and protein, and it serves as the site of…
Q: ICH one is the next tRNA that will arrive to the "A" site of this ribosome? 000000 Gly Arg Glu Pro…
A: The A site is where the next tRNA molecule carrying an amino acid binds to the mRNA. The tRNA…
Q: After the complete ribosome is assembled, what is the first amino-acyl tRNA to enter the ribosome's…
A: In the process of protein synthesis, ribosomes play a crucial role by facilitating the translation…
Q: Think about a ribosome that has already created the dipeptide Met-Ala and is in the process of…
A: Translation is the process of converting the mRNA to proteins Proteins are made of amino acids. The…
Q: In bacteria which ribozyme catalyzes synthesis of peptide bonds between amino acids? 16S rRNA 5S…
A: the translation is the process by which the messenger rna is converted into polypeptide .
Q: the product in a riboprobe transcription reaction is called
A: Riboprobe can be generated by using a polymerase chain reaction (PCR) more quickly and accurately.…
Q: vhich of these molecules is responsible for bringing the correct amino acid to the ribosome? O TRNA…
A: The translation is the process in which the protein is formed from the mRNA. It is the process in…
Q: Synthesis of ribosomal RNA takes place in which of the following eukaryotic cell locations? the…
A: Eukaryotes are the organisms in which nucleus id developed and is surrounded by a membrane.…
Q: What type of cytopathic effect is seen when rabies virus infects a monolayer of cells? O the…
A: The cytopathic effect of the rabies virus on a monolayer of cells is characterized by the formation…
Q: Which part of the ribosome in bacteria, forms the catalytic site for peptide bond formation? 16S…
A: Gene is a hereditary units which is exhibited on the chromosome . Gene expression is a phenomenon in…
Q: For any antibiotic compounds that don’t appear to inhibit translation of proteins from the ribosome,…
A: Antibiotics that target translation interfere with the ribosome's assembly or processing.
Q: Based on the diagram, what can you conclude about how the chloramphenicol behaves as an antibiotic?
A: Chloramphenicol is a broad-spectrum antibiotic whose spectrum includes several gram-positive and…
Q: Which of the following statements about ribosomes is true? Eukaryotic ribosomes have a P site,…
A: Ribosomes are the cell organelle that helps in the process of translation. The structure of…
Q: A eukaryotic region consisting of a combination of enhancer and insulator elements O Ribosome…
A: The correct option is Mediator. Explaination: Cell- and/or cell cycle-specific regulation and…
Q: Once the large ribosomal subunit joins the charged tRNA is at the A site the charged tRNA…
A:
Q: The P site of a ribosome does which of the following? It holds the tRNA carrying the growing…
A: The p-site is known as the peptidyl site and the A-site is the acceptor site which binds to the…
Q: To start translation the ribosome first needs to find the correct end of the transcript. How is that…
A: Translation is the third and final stage of gene expression where the mRNA is read by the adapter…
Q: The synthesis of a protein requires that the amino acids that constitute the growing polypeptide…
A: In the intricate dance of cellular processes, protein synthesis takes center stage, orchestrating…
Q: Which of the groups of introns are self-catalytic (ribozymes)? Groups 1, 2 and 3 O Groups 2 and 3…
A: Group 1
Q: How do sigma factors help regulate gene expression during the transition to stationary phase? O…
A: These are multiple choice questions.
Q: Where in a eukaryotic cell is mRNA made? In the Golgi apparatus In the cytosol In the plasma…
A: In a eukaryotic cell is mRNA made in the nucleus. mRNA is synthesized in the nucleus using the…
Q: Ribosome Amino Acid Ribosome large subunit TRNA UCUAGAG MRNA Ribosome small subunit Figure:…
A: After the process of transcription, mRNA is formed which is translated into protein molecules by the…
Q: The 3 sites that bind tRNAs on a ribosome are on the A, P and E sites. How many sites can tRNA(s) be…
A: Translation is the formation of protein from mRNA. It occurs in cytoplasm of cell.
Q: Polypeptides are synthesized in the amino (NH,) terminus to carboxy terminus (COOH) direction…
A: The Central Dogma concept states that DNA makes RNA and RNA makes proteins. The three most important…
Q: What section in the ribosome will the first anticodon enter? E site A site P site
A: There are specific sites present in the ribosome 1) A site 2) p site 3,) E site
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- Figure 15.16 Many antibiotics inhibit bacterial protein synthesis. For example, tetracycline blocks the A site on the bacterial ribosome, and chloramphenicol blocks peptidyl transfer. What specific effect would you expect each of these antibiotics to have on protein synthesis? Tetracycline would directly affect: tRNA binding to the ribosome ribosome assembly growth of the protein chain Chloramphenicol would directly affect tRNA binding to the ribosome ribosome assembly growth of the protein chainGiven the following mRNA, write the double-stranded DNA segment that served as the template. Indicate both the 5 and the 3 ends of both DNA strands. Also write out the tRNA anticodons and the amino acid sequence of the protein encoded by the mRNA message. DNA: mRNA: 5-CCGCAUGUUCAGUGGGCGUAAACACUGA-3 protein: tRNA:Given the following tRNA anticodon sequence, derive the mRNA and the DNA template strand. Also, write out the amino acid sequence of the protein encoded by this message. tRNA: UAC UCU CGA GGC mRNA: protein: How many hydrogen bonds would be present in the DNA segment?
- The Consequences of Ribosome Complexity Eukaryotic ribosomes are larger and more complex than prokaryotic ribosomal. What advantages and disadvantages might this greater ribosomal complexity bring to a eukaryotic cell?A certain mRNA strand has the following nucleotide sequence: 5AUGACGUAUAACUUU3 What is the anticodon for each codon? What is the amino acid sequence of the polypeptide? (Use Figure 13-5 to help answer this question.) Figure 13-5 The genetic code The genetic code specifies all possible combinations of the three bases that compose codons in mRNA. Of the 64 possible codons, 61 specify amino acids (see Figure 3-17 for an explanation of abbreviations). The codon AUG specifies the amino acid methionine and also signals the ribosome to initiate translation (start). Three codonsUAA, UGA, and UAGdo not specify amino acids; they terminate polypeptide synthesis (stop).A scientist introduces a mutation that makes the 60S ribosomal subunit nonfunctional in a human cell line. What would be the predicted effect on translation? Translation stalls after the initiation AUG codon is identified The ribosome cannot catalyze the formation of peptide bonds between the tRNAs in the A and P sites The ribosome cannot interact with mRNAs tRNAs cannot exit the E site of the ribosome.
- RIPs as Cancer Drugs Researchers are taking a page from the structure-function relationship of RIPs in their quest for cancer treatments. The most toxic RIPs, remember, have one domain that interferes with ribosomes, and another that carries them into cells. Melissa Cheung and her colleagues incorporated a peptide that binds to skin cancer cells into the enzymatic part of an RIP, the E. coli Shiga-like toxin. The researchers created a new RIP that specifically kills .skin cancer cells, which are notoriously resistant to established therapies. Some of their results are shown in FIGURE 9.17. FIGURE 9.17 Effect of an engineered RIP on cancer cells. The model on the left shows the enzyme portion of E. coli Shiga-like toxin engineered to carry a small sequence of amino acids (in blue) that targets skin cancer cells. (Red indicates the active site.) The graph on the right shows the effect of this engineered RIP on human cancer cells of the skin (); breast () liver (); and prostate (). At what concentration of RIP did all of the different kinds of cells survive?RIPs as Cancer Drugs Researchers are taking a page from the structure-function relationship of RIPs in their quest for cancer treatments. The most toxic RIPs, remember, have one domain that interferes with ribosomes, and another that carries them into cells. Melissa Cheung and her colleagues incorporated a peptide that binds to skin cancer cells into the enzymatic part of an RIP, the E. coli Shiga-like toxin. The researchers created a new RIP that specifically kills skin cancer cells, which are notoriously resistant to established therapies. Some of their results are shown in FIGURE 9.17. FIGURE 9.17 Effect of an engineered RIP on cancer cells. The model on the left shows the enzyme portion of E. coli Shiga-like toxin engineered to carry a small sequence of amino acids (in blue) that targets skin cancer cells. (Red indicates the active site.) The graph on the right shows the effect of this engineered RIP on human cancer cells of the skin (); breast () liver (); and prostate (). Which cells survived best at 1 microgram per liter RIP?RIPs as Cancer Drugs Researchers are taking a page from the structure-function relationship of RIPs in their quest for cancer treatments. The most toxic RIPs, remember, have one domain that interferes with ribosomes, and another that carries them into cells. Melissa Cheung and her colleagues incorporated a peptide that binds to skin cancer cells into the enzymatic part of an RIP, the E. coli Shiga-like toxin. The researchers created a new RIP that specifically kills skin cancer cells, which are notoriously resistant to established therapies. Some of their results are shown in FIGURE 9.17. FIGURE 9.17 Effect of an engineered RIP on cancer cells. The model on the left shows the enzyme portion of E. coli Shiga-like toxin engineered to carry a small sequence of amino acids (in blue) that targets skin cancer cells. (Red indicates the active site.) The graph on the right shows the effect of this engineered RIP on human cancer cells of the skin (); breast () liver (); and prostate (). Why are some of the data points linked by curved lines?
- 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 nucleotide sequence of mRNA is converted into the amino acid sequence of a protein. Questions Why is targeting protein synthesis an effective strategy for preventing infection?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 nucleotide sequence of mRNA is converted into the amino acid sequence of a protein. Questions Why are antibiotics ineffective in treating the common cold and other virus infections?Watch this video (http://openstaxcollege.org/l/ribosome) to learn about ribosomes. The ribosome binds to the mRNA molecule to start translation of its code into a protein. What happens to the small and large ribosomal subunits at the end of translation?
