The HbβS(sickle-cell) allele of the human β-globingene changes the sixth amino acid in the β-globinchain from glutamic acid to valine. In HbβC, the sixthamino acid in β-globin is changed from glutamic acidto lysine. What would be the order of these two mutations within the map of the β-globin gene?
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The HbβS
(sickle-cell) allele of the human β-globin
gene changes the sixth amino acid in the β-globin
chain from glutamic acid to valine. In HbβC, the sixth
amino acid in β-globin is changed from glutamic acid
to lysine. What would be the order of these two mutations within the map of the β-globin gene?
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- In Figure 12-4, certain mutations decrease the relativetranscription rate of the β-globin gene. Where are thesemutations located, and how do they exert their effects ontranscription?A normal hemoglobin protein has a glutamic acid at position 6; in sickle-cell hemoglobin, this glutamic acid has been replaced by a valine. List all the possible mRNA codons that could be present for each type of hemoglobin. Can a single base change result in a change from Glu to Val in hemoglobin?You have the following DNA coding sequence of a wild-type allele: 5’-ATG TTC CAG CTA GAT GAT ATG CTG GTA ATT GGG GAA CGC GCG CGG TAA-3’ For each of the following mutations: A. State whether the mutation is missense, nonsense, frameshift, or silent. B. Write the codon change that occurs for the missense, nonsense, and silent mutations (ex. GAA -- GAT). C. For frameshift mutations, write out the entire mutant sequence with each codon clearly indicated (if the frameshift creates a new stop codon, end the sequence at the new stop). Using the wild type DNA sequence above as a guide : Write the amino acid sequence of the mutants. Mutant 1: transition at nucleotide 23 Mutant 2: T --> G transversion at nucleotide 29 Mutant 3: an insertion of “A” after nucleotide 14 Mutant 4: transition at nucleotide 7 Mutant 5: An insertion of GG after nucleotide 40 Mutant 6: transition at nucleotide 15 Mutant 7: a deletion of nucleotide 25
- Shown below are two homologous lengths of the alpha and betachains of human hemoglobin. Consult a genetic code dictionary and determine how many amino acid substitutionsmay have occurred as a result of a single nucleotidesubstitution. For any that cannot occur as a result of a singlechange, determine the minimal mutational distance. Alpha: ala val ala his val asp asp met proBeta: gly leu ala his leu asp asn leu lysLeber Congenital Amaurosis (LCA) causes progressive vision loss due to defects in the gene that encodes RPE65 isomerase. Affected individuals are homozygous recessive for mutant alleles of the RPE65 gene. You are trying to determine the molecular nature of the mutations in three individuals with LCA. For ease of analysis, you may assume that each individual is homozygous for the same mutant allele (though the three individuals have different mutations than each other). You use the polymerase chain reaction to amplify DNA from each patient and you determine the sequence of the DNA and compare it to unaffected individuals. You identify the following differences. Note that the non-template strand of DNA is given and the changes are highlighted using red boldface. You can assume that the sequences are in the first reading frame (eg. the first three nucleotides of each sequence is a codon). The coding region of the gene is 1602 bp and the position of the sequences shown below is…The protein encoded by the cystic fibrosis gene is 1480amino acids long, yet the gene spans 250 kb. How is thisdifference possible?
- Proteins A,B,C, and D in the diagram are encoded by different genes and interact with each other. Imagine that a mutation in the gene for protein A changes one of the charged amino acid in the red circle area from positive to negative charge (blue arrow). this mutation results in a mutant phenotype. Assume a mutation in the gene for protein B occurs and the double mutants have a phenotype that is almost wild type. How would you best describe the mutation in gene B? Protein C Proten A Protein B Protein B Wild type Mutation in the gene for protein AThe proximal histidine residues have been replaced by glycine residues by mutation of the cloned genes for both the α and β subunits of hemoglobin. With the tetrameric mutant hemoglobin (all subunits being mutant, α H F8 G, β H F8 G), it was found that the “proximal” coordination bonds to hemes in the mutant protein could be replaced by having the small molecule imidazole in the buffers. Oxygen binding curves for the tetrameric mutant hemoglobin were measured. A. The degree of cooperativity in oxygen binding for the mutant hemoglobin (with imidazole present) would be expected to 1) increase 2) decrease 3) not be affected) compared with the normal protein. B. Justify your answer to part A in terms of what you know about the structural basis of cooperativity in hemoglobin. C. How would the Hill coefficient for the mutant be expected to change compared with nH for normal hemoglobin, which is ~3?Two missense mutations in the gene that encodes an enzyme called superoxide dismutase cause a form of amyotrophic lateral sclerosis (ALS, or Lou Gehrig disease). This disease causes loss of neurological function over a 5-year period. One mutation alters the amino acid asparagine (Asn) to lysine (Lys). The other changes an isoleucine (Ile) to a threonine (Thr). List the codons involved and describe how single-base mutations can alter the specified amino acids.
- The genetic alteration responsible for sickle-cell anemia in humans involves: a transition mutation from A to G, substituting glutamic acid for valine in a-globin a transversion mutation from T to A, substituting valine for glutamic acid in b-globin a transition mutation from T to C, substituting valine for glutamic acid in b-globin a transversion mutation from G to C, substituting glutamic acid for valine in a-globin a frameshift mutation of one ATC codon, removing glutamic acid from b-globinYou have created three different mutations in the histoneH1 protein (HISmut1, HISmut2, HISmut3), and each of these mutations eliminate a stretch of 5 amino acids from the primary sequence. Based on the description of where you find the mutant histoneH1 proteins when you look inside a cell in each of the cases below, describe 1) what the function is of the amino acids that were removed, and 2) what is not happening with the mutant histoneH1 protein that does happen with wild type H1: 1. HISmut2 protein is found in the cytoplasm, and never in the nucleus. 2. HISmut1 protein is found in only briefly in the cytoplasm because it is very quickly sent to the proteasome. 3. HISmut3 protein is found floating freely throughout the nucleoplasm.You are interested in studying a unique protein found in a rare wildflower found in the desert region of Atacama. The wild-type amino acid sequence isolated from this flower is: Wildtype: Arg-Lys-Thr-Leu-Gly-Arg A mutant for the gene that specifies this protein is isolated and the amino acid sequence of its protein is determined: Mutant: Arg-Lys-Thr-Leu-Gly-Gly a) Identity what the mutation changed in the amino acid sequence b) What is the effect of the mutation at the amino acid level? c) What is the effect of the mutation at the RNA level? d) What kind of mutation happened at the DNA level?