Can someone please help me or point me in the right direction. Willing to donate!!
1. A strain of E. coli carries a substitution mutation causing the terminator codon 5’-UAG-3’ to occur at an interior position in a particular type of mRNA. This strain also carries a suppressor mutation that alters the anti-codon of a type of tRNA molecule so that it reads 3’-AUC-5’. This type of tRNA reads this terminator codon and inserts the amino acid tyrosine.
a. What effect would the presence of both of these mutations together have on the polypeptide translated from the mRNA carrying the mutant terminator codon?
b. Do you expect that there might be other genes whose translation would be altered by the presence of the tRNA produced by this suppressor gene? If so, describe the circumstances under which translation would be altered and explain how it would be altered.
2. A gene in a haploid organism produces an mRNA transcript containing a section with three adjacent codons that are identical and that code for leucine. Sequencing mRNA from the same gene following exposure of the organism to a mutagenic chemical indicates that codons at these three sites now code for tryptophan, serine, and lucine. Assume that the mutations that occurred were single-base substitutions. What was the makeup of the codons present in the original mRNA?
3. Human hemoglobin is a complex protein molecule made up of four poly-peptides joined to an iron-containing heme group. In normal human adult haemoglobin, hemoglobin A, or HbA, two kinds of polypeptides designated as alpha and beta are found. Two identical alpha and two identical beta chains plus the heme group make up each molecule of haemoglobin A. Hemoglobin S, or HbS, is a haemoglobin variant occurring in individuals affected with the heritable disorder sickle cell anemia. A comparison of the amino acid sequences of the polypeptides in hemoglobins A and S indicates that the alpha chains in the two molecules are identical , but that the beta chains differ in a single interior amino acid.
a. How many kinds of genes are necessary for the synthesis of haemoglobin S?
b. Assuming that the gene for the beta chain of HbS arose from the gene for the beta chain of HbA through a single mutation, what general type of mutation was most likely responsible?
c. The difference between the beta chains of haemoglobin S and A is restricted to the sixth amino acid from the amino (-NH2) end of the polypeptide. In haemoglobin S, the amino acid at the site is valine and in haemoglobin A it is glutamic acid. From your knowledge of the genetic code (and with reference to the genetic code) what can you deduce about the specific (and simplest) base alteration in the beta polypeptide that would produce the amino acid substitution.