Essentials of Genetics (9th Edition) - Standalone book
9th Edition
ISBN: 9780134047799
Author: William S. Klug, Michael R. Cummings, Charlotte A. Spencer, Michael A. Palladino
Publisher: PEARSON
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Chapter 12, Problem 9PDQ
Summary Introduction
To review:
In the studies of the sequence of amino acid of wild-type as well as mutant forms of tryptophan synthetase in Escherichia coli(E.coli), the changes shown below have been observed:
Determine the set of triplets (codons) in which only one
Introduction:
Tryptophan synthetase is an enzyme that is involved in the biosysnthesis of tryptophan. It is mainly found in microorganisms such as E.coli. It is not present in animals. This is coded by different nucleotide bases corresponding to specific amino acids.
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For E. coli strains with the lac genotypes show below, use a plus sign (+) to indicate the synthesis of β-galactosidase and permease and a minus sign (–) to indicate no synthesis of the proteins.
1.
a)What would happen if the aminoacyl tRNA synthetase responsible for charging alanine tRNAs also charged methionine tRNAs with alanine?
b)What would happen if an individual was homozygous for mutant alleles of the gene encoding the aminoacyl tRNA synthetase responsible for charging leucine tRNAs?
Neurospora crassa can synthesize the amino acid arginine from a
precursor as follows:
precursor
ornithine - citrulline arginine
George Beadle and Edward Tatum identified various mutants (arg
mutants) unable to synthesize arginine from this precursor. One such
class (Class I) could synthesize arginine if either ornithine or citrulline
was supplied. A second mutant class (Class II) could synthesize
arginine if citrulline was added, but not if ornithine was added. A
third class (Class II) could not synthesize arginine from either
ornithine or citrulline.
Which class or classes of arg mutants LACK a functional enzyme
able to convert ornithine into citrulline?
Chapter 12 Solutions
Essentials of Genetics (9th Edition) - Standalone book
Ch. 12 - CASE STUDY | A drug that sometimes works A...Ch. 12 -
CASE STUDY | A drug that sometimes works
A...Ch. 12 -
CASE STUDY | A drug that sometimes works
A...Ch. 12 - HOW DO WE KNOW? In this chapter, we focused on the...Ch. 12 - Review the Chapter Concepts list on p. 215. These...Ch. 12 - In studies of frameshift mutations, Crick,...Ch. 12 -
4. The mRNA formed from the repeating...Ch. 12 - In studies using repeating copolymers, AC......Ch. 12 - Prob. 6PDQCh. 12 - Prob. 7PDQ
Ch. 12 -
8. When the amino acid sequences of insulin...Ch. 12 - Prob. 9PDQCh. 12 - Why doesn't polynucleotide phosphorylase (Ochoa's...Ch. 12 - Refer to Table 12.1. Can you hypothesize why a...Ch. 12 -
12. Predict the amino acid sequence produced...Ch. 12 - A short RNA molecule was isolated that...Ch. 12 - A glycine residue exists at position 210 of the...Ch. 12 - Shown here is a theoretical viral mRNA sequence...Ch. 12 -
16. Most proteins have more leucine than...Ch. 12 - Define the process of transcription. Where does...Ch. 12 - Describe the structure of RNA polymerase in...Ch. 12 - In a written paragraph, describe the abbreviated...Ch. 12 - Messenger RNA molecules are very difficult to...Ch. 12 - One form of posttranscriptional modification of...Ch. 12 - In a mixed copolymer experiment, messages were...Ch. 12 -
23. Shown in this problem are the amino acid...Ch. 12 - Alternative splicing is a common mechanism for...Ch. 12 - The genetic code is degenerate. Amino acids are...
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- A glycine residue is in position 210 of the tryptophan synthetase enzyme of wild-type E. coli. If the codon specifying glycine is GGA, how many single-base substitutions will result in an amino acid substitution at position 210? What are they? How many will result if the wild-type codon is GGU?arrow_forwardThe enzyme dihydrofolate oxidase has 3 adjacent asparagines residues (codon for asparagines is ACC): explain how site directed mutagenesis could be used to increase the thermal stability of the proteinarrow_forwardA mutant has no activity for the enzyme isocitrate lyase.Does this result prove that the mutation is in the geneencoding isocitrate lyase?arrow_forward
- Consider the mechanism of the enzyme RNase: What would happen to the Km (i.e., would it increase, decrease, or stay the same) if the his12 was mutated to a lysine? Explain. What would happen to the Kcat (i.e., would it increase, decrease, or stay the same) if the his12 was mutated to a valine? Explain.arrow_forwardSeveral genes code for enzymes that are responsible for histidine biosynthesis in Escherichia coli. Part of the nucleotide sequence of the gene that codes for one of these enzymes is: AUG CCU UGG GCC CAA AAA UGC A series of mutants that have lost activity for this enzyme are recovered. The mutant products are analyzed and found to have the following amino acid sequences: Mutant 1: Met-Pro-Trp-Pro-Glu-Lys-Cys Mutant 2: Met-Pro Mutant 3: Met-Pro-Cys-Gly-Pro-Lys-Met Mutant 4: Met-Pro-Trp-Pro-Lys-Asp Choose the correct type of mutation that occurred in the DNA to produce each mutant type. Nonsense Answer Missense Answer Addition Answer Deletion Answerarrow_forwardThe authors state: "Properties of the single mutants K557R, D591V and K617A, a double mutant, D591V/K617A, and a triple mutant, K557R/D591V/K617A, were evaluated to find an allosteric binding site for citrate." The numbers between the letters represent the residue number altered. The letter in front was the wild type and the letter afterwards is the mutant. How would the the triple mutations K557R and D591V and K617A alter the overall protein? O lower the # of charges, increase the pl O increase the # of charges, increase the pl O lower the # of charges, lower the pl O lower the # of charges, increase the pl O no change in the # of charges, increase the pl O no change in the # of charges, lower the plarrow_forward
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