4. Compare regulation by allosteric control, reversible covalent modification, andproteolytic activation strategies. When might one strategy be more useful than another?

Enzymes are high molecular-weight proteins that catalyse biochemical reactions. They are also called…

Answered: 4. Compare regulation by allosteric…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Metabolic control is crucial part of survival for all bacteria. The lactose operon is located on the bacteria chromosome and assists in maintaining homeostasis. (l) Describe how an operon regulates the expression of genes. (m) Feedback plays an important part in life helping to maintain homeostasis. Explain how both negative and positive feedback help maintain homeostasis
Like the lac operon, the hexose operon is controlled by a separate regulatory protein under the control of its own promoter (see the schematic of the operon below). The hexose regulatory protein is sensitive to fatty acyl CoA levels. When all hexose fuel sources are depleted, the bacteria switch to lipid metabolism and fatty acyl CoA levels increase. This turns expression of the hexose operon off. +1 +1 Regulatory Gene Pregulator Hexose Operon Genes operon regulator promoter operon promoter 5e. The regulatory protein that controls expression of the hexose operons is a transcriptional ACTIVTOR or REPRESSOR (circle one).
1. You are interested in the eukaryotic protein/enzyme Thiolase, which is 200 amino acids in length. Because Thiolase is only active in the peroxisome (an organelle) you know there must be a peroxisomal localization signal sequence in the protein. Sub-cellular Location Construct of GFP protein In order to be able to visualize the Thiolase protein in a cell, you create a fusion Cytosol construct with the gene for Thiolase and the GFP gene for Green Fluorescent Protein (GFP). 200 Thiolase Peroxisome GFP You also make a series of deletions in the 50 200 Peroxisome gene for Thiolase, all fused with the GFP GFP 100 200 gene. Numbers on top of the constructs GFP Peroxisome represent amino acid positions. 125 200 Cytosol GFP You express each construct in a mammalian 150 200 cell and use a microscope to visualize where the Thiolase-GFP protein gets trafficked. cytosol GEP 150 Peroxisome GFP Using the data provided, where must the peroxisomal localization signal sequence be in the Thiolase…
You plan to synthesize a peptide to be used as a vaccine to treat melanoma, a particularly aggressive form of skin cancer. Normally, gp100, a protein on the surface of melanocytes, activates cell growth when it is bound by its ligand. Activation of the growth pathway depends on the presence of threonine in the ligand. The effective peptide vaccine will mimic the natural ligand, but won’t cause cell growth and division. Below is the sequence of the natural ligand: LDMKTAG In order to ensure your newly designed peptide vaccine does not cause cell growth upon binding, you must substitute the Threonine residue at position 5. What amino acid would you replace it with, bearing in mind that the peptide should still be similar enough to bind to the gp100 protein in the surface of melanocytes. Explain your choice. Your vaccine will be administered as a topical cream, and you require your peptide to have an overall neutral charge in order to be functional. At what pH should you formulate…
3. Consider the pathway for the synthesis of the amino acid arginine in Neurospora: ARG-F. → ARG-E → citrulline ARG-H ornithine Mutant strains of Neurospora are grown in minimal media supplements as follows. Each mutant strain carries only a single mutation. Growth is shown by (+), no growth is shown by (o). → argininosuccinate > arginine Supplements citrulline arginino- succinate mutant nothing Qraitibine arginine strain +. Indicate the correct strain / defective gene pairing. a) strain a / ARG-F b) strain a/ ARG-H strain b / ARG-F d) strain c / ARG-E e) strain c / ARG-F + + +
4A. Write out the chemical equations (structures are not necessary) for the two steps in the reaction catalyzed by aminoacyl tRNA transferase. Include all products and reactants. Step 1: amino acid activation Step 2: aminoacyl transfer to the tRNA 4B. Write the chemical equation for the net reaction catalyzed by aminoacyl transferase. This can be determined by taking the sum of the two reactions above.
1. What are two major similarities between protein synthesis in bacteria and eukaryotes? What aretwo major differences? 2. Is it reasonable to expect that protein degradation can take place at any location in a cell? 3. . In ubiquitination, chaperone can be part of the process. Explain the benefits of using chaperoneand differentiate the uses of chaperone and ubiquitin.
2. Below, recognition sites of two of these enzymes, Pstl and Nsil, are given 5'... CTGC AG. 3... GACGTC...5 3 Pstl recognition and cleavage site 5... ATGCAT 3'... TACGTA ... 5' 3' ... Nsil recognition and cleavage site a. Does cleavage by Pstl result in a 5' or 3' overhang? What is the sequence of this overhang? b. Does cleavage by Nsil result in a 5' or 3' overhang? What is the sequence of this overhang? c. Suppose you have a cloning vector that contains a Pstl recognition site and you also have foreign DNA that was cut with Nsil. Can this DNA be ligated into the Pstl site of the vector, and if so, explain its reason and draw the new ligation site. d. Can the new ligated DNA segment sequence be cut from the vector with Pstl or Nsil ? What potential problems do you see?
Please draw a concept map using the following terms for regulation Repressor, Inducer, Induction, Negative regulation, Repression, Operator, Positive Regulation, Activator, Sigma-32, Sensor Kinase, Two-componenet Regulation, Lac operon, Heat shock, Catabolite repression, trp operon, Feedback inhibition, Protein Stability, Sigma factors, Response regulator, Riboswitch, Homoserine Lactone, Quorum sensing, Autoinducing Peptide, RNA regulation, Antisense RNA
4.) Fully explain the role Gal3 has in the expression of galactose inducible (gal) genes.
Hello, no need for explination just say which option, thanks.
Distinguish between positive and negative control. Give examples of each from the lac operon

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4. Compare regulation by allosteric control, reversible covalent modification, and proteolytic activation strategies. When might one strategy be more useful than another?