4. Please propose an experimental design to address the following hypothesis: Eukaryotic initiation factor 4E (EIF4E) binds eukaryotic initiation factor 4G (elF4G) inside cells.
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Q: double-stranded RNA
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- 2. Several techniques were used to study the degree of translocation of truncated intermediates in the synthesis of an integral membrane protein (with a single transmembrane domain). Experiments were performed in the presence of SRP and canine pancreatic microsomes. The intermediates were synthesized using a rabbit reticulocyte translation system in the presence of 35S-methionine. Of the techniques used to monitor the progress of synthesis and translocation/insertion,| we are concerned with the following: Sedimentation: chains associated with the microsomes are found in the pellet of a 75,000 rpm ultracentrifuge spin. Crosslinks: a photoreactive phenylalanine derivative was incorporated into the truncated chain, and crosslinking to protein and lipid was analyzed after photo-activation. The intermediates studied using these approaches had between 40 and 154 amino acids. All truncated proteins with more than 60 amino acids sediment by centrifugation at neutral pH, while only…10. In eukaryotic cells, glycosylation activity of membrane proteins is found in the lumen of the endoplasmic reticulum (ER) and is accomplished by the enzyme oligosaccharyl transferase (OST), which adds oligosaccharides to the amino group of Asn residues of the consensus sequence Asn-X-Thr/Ser. a. The following ER membrane protein construct has a cytosolic N-terminal region and a membrane-spanning variable sequence. The variable sequence is a signal anchor (SA) sequence. Would you expect the C-terminal region of the B subunit to be glycosylated? Why or why not? variable sequence C-terminal region of B-subunit N-terminal region b. An additional transmembrane region is added to the construct prior to the variable sequence, as shown below. The transmembrane is a signal anchor (SA) sequence, while the variable sequence is a stop transfer anchor (STA) sequence. Would you expect the C-terminal region of the B subunit to be glycosylated? Why or why not? C-terminal region of B-subunit…3). Consider the four mutations (i-iv) described below: i. One of the mutations causing cystic fibrosis in humans is a deletion of three nucleotides that eliminates a phenylalanine at position 508 of the CFTR protein (D508). Normally, CFTR protein is localized to the plasma membrane, where it functions as a chloride ion channel. D508 CFTR is misfolded and all of it is degraded without ever reaching the cell surface. ii. The yeast transcription factor Gal4p contains a DNA-binding domain and a transcriptional activation domain. An allele with a deletion the gene portion encoding the activation domain encodes a truncated Gal4p containing only the DNA-binding domain. It binds to Gal4p target genes at appropriate binding sites in their upstream regulatory regions, but does not activate their transcription. In cells with both wild type and mutant forms of Gal4p, the truncated Gal4p binds more efficiently to target DNA sequences than wild type. iii. Mutations in the acid maltase gene in…
- 7) Please propose a mechanism that may link the increased abundance of unfolded proteins(perhaps due to elevated temperatures) with increased ability of the cell to facilitateprotein folding. The mechanism should involve a sequence of multiple events.1. why is the ribosome a good drug target? 2. Tetracyclines: a. Where do first generation tetracyclines bind? b. Which step in protein translation do they inhibit? C. Why was it necessary to come out with a third generation tetracycline, and how are they different? 3. What are three ways that 2-deoxystreptamine (2-DOS) aminoglycosides can inhibit protein synthesis? 4. Chloramphenicol: a. Where does this drug bind? b. How does it inhibit protein synthesis?1)You add a drug to cells that can pass through hydrophilic or hydrobic environments (e.g., membranes & cytosol). The drug specifically prevents the binding of KDEL (ER retention signal) to any other molecules. In the short term, what would happen to the synthesis and localization of translocon proteins? a. New complete translocon proteins would be made, but they would end up in the golgi apparatus. b. New complete translocon proteins would be made, but they would end up at the plasma membrane c. No new intact translocon proteins would be synthesized d. New complete translocon proteins would be made, but they would be secreted e. New complete translocon proteins would be made and localized normally
- 1. The SARS-CoV-2 virus (causing Covid-19) has an RNA genome, which is replicated using an RNA-dependent RNA polymerase (RdRp). The structure below shows a drug that was recently developed as a treatment for infection with SARS-CoV-2 (a) Which molecule normally found in a cell does it most resemble? (You can ignore the part of the structure highlighted with a red box. This is removed by hydrolysis when the drug enters the cell). (b) Suggest a mechanism by which this molecule might inhibit infection. (c) Why is this drug unlikely to have major effects in the host? HN OH OH97Which of the following is examples of a transposable element found in bacteria? (multiple choice questions)A.IS903b.Tn5c.IS1D.Xis 98What is the key component of the catalytic site of the spliceosome? (multiple choice questions)A.DNAb.ribosomesc.proteinD.RNA 99Which antibiotic can binds to RNA polymerase and blocks an early step in RNA synthesis?A.Ampicillinb.Chloramphenicolc.RimantidineD.None of the above 100All tRNA molecules have poly (A) tails at their 3' end. Yesorno1. (a) By binding one L-tryptophan molecule/monomer, the trp repressor binds to DNA to sup- press synthesis of L-tryptophan in E. coli. Below is the amino acid sequence of the helix - reverse turn - helix region of the trp repressor that binds to DNA compared to the sequence of the corresponding DNA binding motif of the Prl protein. A diagram of the trp repressor dimer is also shown. Trp Prl Trp Prl 80 -Gly-Glu-Met-Ser-Gln-Arg-Glu-Leu-Lys-Asn-Glu-Leu-Gly-Ala-Gly-Ile- -Ser-Glu-Glu-Ala-Lys-Glu-Glu-Leu-Ala-Lys-Lys-Cys-Gly-Ile-Thr-Val- trp helix 5 70 trp helix 4 Prl helix 80 Prl helix Ala-Thr-Ile-Thr-Arg-Gly-Ser-Asn-Ser-Leu-Lys-Ala-Ala- Ser-Gln-Val-Ser-Asn-Trp-Phe-Gly-Asn-Lys-Arg-Ile-Arg- reverse turn 90 Comparing the two protein sequences above, identify all amino acid pairs that differ in electrostatic charge due to proton dissociable groups (assume pH 7). Indicate the charge of both residues for each such pair. (b) Circle the pair of residues for which the electrostatic charge due to…
- Part A Shown above is a schematic diagram of the E. coli leader peptidase (Lep) which has several basic amino acids in a cytoplasmic loop. Propose a mutant of Lep that would be a test of the "inside positive" rule for the orientation of proteins in membranes. Match the words in the left column to the appropriate blanks in the sentences on the right. Make certain each sentence is complete before submitting your answer. terminal reversed same (+) (-) center 1. Make mutant Lep that substitutes noncharged residues for the chains in the loop, and put charged side chains in 2. If the inside-positive rule applies, the mutant ought to have the membrane. Reset Help charged side positions. orientation in the1. Describe the process by which an integral membrane glycoprotein goes from mRNA to being an integral membrane protein 2. Describe in detail the initiation of translation in eukaryotes versus prokaryotes. All steps. 3. Compare and contrast gated transport and transmembrane transport of mitochondria. Specific details are required. 4. Compare and contrast regulation of gene expression between prokaryotes and eukaryotes 5. The plasma membrane, as an example, is described as a fluid mosaic. Why? (hint: LOTS of details)3. A student in my lab was trying to express the cytosolic (not membrane bound) enzyme PseG and decided to express the enzyme as a Hisí fusion (PseG-His) to ease purification. In his initial experiments, he (1) expressed the protein in bacterial cells (E. coli), (2) lysed the bacteria using a gentle lysis buffer (one that would solubilize folded proteins), and (3) assessed the protein's presence in whole-cells (WC) pre-lysis, and pellet (P) versus soluble (S) cell fractions post-lysis, by SDS-PAGE analysis. In his first expression experiment, he collected the data shown in Figure 1: kD 58 46 kD MW WC PP 175 80 58 46 30 25 │I T||| || | 10- Coomassie-stained protein gel a. From these initial data, what can you conclude about the following features of PseG-His6 in E. coli? Expressed? Soluble? Folded? 10->> In a follow-up experiment, my student (1) expressed the protein in bacterial cells (E. coli), (2) lysed the bacteria using a harsh lysis buffer that included 6 M urea (a detergent), and…