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Question: 5. You Are Studying Mutations In A Gene That Codes For An Enzyme Whose Amino Acid Sequence Is Known. The Gene In The Wild Type Strain (WT) Encodes A Protein Where Tyrosine (Tyr, Y) Is The Tenth Amino Acid From The Amino Terminal End. You Mutagenize WT. You Recover A Mutant Strain (MT) In Which You Find A Cysteine (Cys, C) At Position 10. You Subject …

Question: 5. You Are Studying Mutations In A Gene That Codes For An Enzyme Whose Amino Acid Sequence Is Known. The Gene In The Wild Type Strain (WT) Encodes A Protein Where Tyrosine (Tyr, Y) Is The Tenth Amino Acid From The Amino Terminal End. You Mutagenize WT. You Recover A Mutant Strain (MT) In Which You Find A Cysteine (Cys, C) At Position 10. You Subject …

please complete all the part (part A please fill thediagram).

5. You are studying mutations in a gene that codes for an enzyme whose amino acid sequence is known. The gene in the Wild Typ

b. Assume amino acid 10 is important for the function of the active site. Would the enzyme produced by MT strain be functionac. Why does the enzyme produced by Strain A behave like WT? Why is the enzyme produced by Strain B non-functional? Explanatio

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5. You are studying mutations in a gene that codes for an enzyme whose amino acid sequence is known. The gene in the Wild Type Strain (WT) encodes a protein where Tyrosine (Tyr, Y) is the tenth amino acid from the amino terminal end. You mutagenize WT. You recover a Mutant Strain (MT) in which you find a Cysteine (Cys, C) at position 10. You subject MT to further mutagenesis and recover three different strains. Strain A has Serine (Ser, S) at amino acid position 10 and acts just like wild type. Strain B has Arginine (Arg, R) at amino acid position 10 and is non-functional. Strain C has no detectable enzyme function at any temperature. With great difficulty, you recover a truncated, nine amino acid polypeptide protein expressed from this gene in strain C. a. The mutagen you used allows only a SINGLE nucleotide substitution. Complete the flowchart below to explain the changes in coding strand DNA for codon 10 from WT to MT to Strains A, B and C. You may only change one base at a time. (5 points) WT strain Y 5′ ATG codons 2-9 … codon 10 MT strain C 5 ATG codons 2-9 … codon 10 S R ? Strain A codons 2-9 Strain B codons 2-9 Strain C codons 2-9 5′ ATG 5′ ATG 5 ATG codon 10 codon 10 codon 10 b. Assume amino acid 10 is important for the function of the active site. Would the enzyme produced by MT strain be functional or not? Explain your answer. (2 points) c. Why does the enzyme produced by Strain A behave like WT? Why is the enzyme produced by Strain B non-functional? Explanation for Strain A (1 point): Explanation for Strain B (1 point): d. Define “nonsense suppressor” mutation. (1 point) e. Strain C was further mutagenized to produce Strain D. The enzyme isolated from Strain D functions just like WT. When you sequence the DNA encoding the gene for this enzyme from Strain D, you see the same mutation in codon 10, as is in Strain C! You are shocked – the Strain C mutation is still there. You use mass spectrometry to determine the amino acid sequence of the polypeptide. You are even more shocked to find Ser at position 10! Dr Mistry says you shouldn’t be shocked. Instead, she tells you to connect your answer in part d with the concept described in Fig 9-18 in your textbook. You are also asked to ignore wobble. Explain what happened. For full points show how the change in the sequence of bases in Strain D permits the incorporation of Ser at position 10 (5 points)




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