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- You are given 3 tubes of RNA and asked by your supervisor to clone the gene encoding the proinsulin C-peptide that will be used later to produce insulin. The first tube contains purified mRNA isolated from pancreatic β-cells from a patient in a post-absorptive state. The second tube contains purified mRNA isolated from pancreatic α-cells from a patient during absorptive state. The third tube contains purified mRNA isolated from pancreatic β-cells from a patient during absorptive state. 1) Which tube from the three is the most appropriate to use and why? 2) Describe the primary procedure (key steps no details) that you will follow to clone the C-peptide gene from the RNA above into the only vector you have, a pUC expression vector cut open using EcoR1 which has a 5¢-recognition site and a 3¢- HindIII in the MCS? 3) How can you guarantee a high expression of your protein in any expression vector?you are given 3 tubes of RNA and asked by your supervisor to clone the gene encoding the proinsulin C-peptide that will be used later to produce insulin. The first tube contains purified mRNA isolated from pancreatic β-cells from a patient in a post-absorptive state. The second tube contains purified mRNA isolated from pancreatic α-cells from a patient during absorptive state. The third tube contains purified mRNA isolated from pancreatic β-cells from a patient during absorptive state. In not more than 2 pages provide answers for the following question? Describe the primary procedure (key steps no details) that you will follow to clone the C-peptide gene from the RNA above into the only vector you have, a pUC expression vector cut open using EcoR1 which has a 5¢-recognition site and a 3¢- HindIII in the MCS?You are given 3 tubes of RNA and asked by your supervisor to clone the gene encoding the proinsulin C-peptide that will be used later to produce insulin. The first tube contains purified mRNA isolated from pancreatic β-cells from a patient in a post-absorptive state. The second tube contains purified mRNA isolated from pancreatic α-cells from a patient during absorptive state. The third tube contains purified mRNA isolated from pancreatic β-cells from a patient during absorptive state. In not morethan 2 pages provide answers for the following questions? 1) Which tube from the three is the most appropriate to use and why? 2) Describe the primary procedure (key steps no details) that you will follow to clone the C-peptide gene from the RNA above into the only vector you have, a pUC expression vector cut open using EcoR1 which has a 5-recognition site and a 3- HindIII in the MCS? 3) How can you guarantee a high expression of your protein in any expression vector?
- You are given 3 tubes of RNA and asked by your supervisor to clone the gene encoding the proinsulin C-peptide that will be used later to produce insulin. The first tube contains purified mRNA isolated from pancreatic β-cells from a patient in a post-absorptive state. The second tube contains purified mRNA isolated from pancreatic α-cells from a patient during the absorptive state. The third tube contains purified mRNA isolated from pancreatic β-cells from a patient during the absorptive state. provide answers to the following questions? 1) Which tube from the three is the most appropriate to use and why? 2) Describe the primary procedure(key steps no details) that you will follow to clone the C-peptide gene from the RNA above into the only vector you have, a pUC expression vector cut open usingEcoR1which has a 5¢-recognition site and a 3¢- HindIII in the MCS? 3) How can you guarantee a high expression of your protein in any expression vector?Which of the following would you expect to happen if there were a mutation in the Iron Response Element (IRE) that prevented IRE-binding proteins from binding to the IRE. The ferritin gene will only be translated with a low concentration of iron The ferritin gene will only be translated with a high concentration of iron The ferritin gene will be translated, regardless of the concentration of iron, The ferritin gene will not be translated, regardless of the concentration of ironHow would a human cell normally change its expression of the gene for tyrosine aminotransferase? adipose cells will turn on this gene in the presence of glucocorticoids liver cells will turn on this gene in the presence of glucocorticoids liver cells will turn on this gene in the absence of glucocorticoids liver cells will turn off this gene in the presence of glucocorticoids adipose cells will turn off this gene in the absence of glucocorticoids
- You are studying growth factor GFA, which you know stimulates the proliferation of goblet cells in theintestine.Goblet cells are responsible for producing and secreting mucin, a mixture of glycosaminoglycans thatprotects the intestinal wall.Some patients suffering from inflammatory bowel disease (IBD) appear to have fewer goblet cells, thereforeless mucin and less protection from toxins and various other pro-inflammatory factors.These patients also have mutations in the gene encoding the GFA receptor (GFAR) in goblet cells,GFAR is a receptor tyrosine kinase (RTK) that autophosphorylates in response to GFA binding, thusbecoming active.QUESTION:explain what changes in GFAR could be caused by these IBD-associatedmutations and why.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?Which of the following statements about the tryptophan operon in E. coli is TRUE? Choose an answer below: It needs an inducer for gene expression. It contains the gene for lactose permease. It has no operator. Its whole regulation is based on attenuation. It contains a leader peptide upstream of the structural genes.
- Lactase is an enzyme in the small intestine that helps break down the sugar lactose, found in milk. As lactose approaches the active site of lactase, as shown in the image, which of the following occurs first? The lactose molecule is broken into glucose and galactose. Lactase shifts to its lowest free energy level to allow lactose to enter the active site. Lactose creates a microenvironment as it approaches lactase to promote binding. Temporary bonding occurs between the active site and the substrate, causing a conformational change.Which of the following statements are true? (check all that apply) □ AHL promotes glycolysis □ Changing the expression level of EsaI changes the timing of AHL production □ The E coli strain without EsaI has higher GFP expression that those with EsaI because glycolysis is turned on. □ The E coli strain without EsaI has higher GFP expression that those with EsaI because the glucaric acid pathway is turned on.