Predict the outcome of two tandem tryptophan codons (UGGUGG) that are mutated to become tryptophan-cysteine codons...

Predict the outcome of two tandem tryptophan codons (UGGUGG) that are mutated to become tryptophan-cysteine codons (UGGUGC)? How would this change affect the regulation of tryptophan biosynthesis? Explain your answer and include the role of the regions within the leader sequence.

Expert Solution

In tryptophan operon regulation, leader sequence plays an important role in switch off or on position. There are 4 regions on mRNA, region 1,2,3 and 4. Region 3 can complement between 2 and 3 both. If region 3 combine with 2 then transcription continous and tryptophan operon become switch on and if 3 complementry with 4 then it's cause hairpin like structure which leads to premature termination of transcription and hence tryptophan is switch off.

If leader sequence are having genetic codon of tryptophan amino acid then during protein synthesis ribosome halt or stop moving ahead when tryptophan absent in cell, due to lack of charged tRNA with tryptophan, so tryptophan operon become switch on.

Now, if tryptophan genetic codon is mutated to cysteine then ribosome does not halt there and hairpin like structure form between sequence no. 3 and 4 on mRNA which leads to pretermination of transcription so operon become switch off even in absence of tryptophan in cell.

Hope it's clear..thanks

gladiator answered 2 years ago

Part A - Short Answer If tryptophan (trp) codons containing two trp codons in its leader...

Part A - Short Answer If tryptophan (trp) codons containing two trp codons in its leader region were mutated to serine (ser) codons, then a high level of expression of the mutated operon would be visible ONLY if trp and ser were absent at the same time from the media. Explain why this occurs. Part B - Multiple Choice Circle the correct relationship between the trp operon and the repressor. The repressor acts in 'cis'. The repressor protein is responsible...

What is the biochemical outcome of Zellweger's (disease) mutated protein? What is the biological consequence of...

What is the biochemical outcome of Zellweger's (disease) mutated protein? What is the biological consequence of the mutation? How does the mutation lead to a defective biochemical pathway that leads to the phenotype? Does the mutations affect the promoter? If so, explain

predict what would happen if the tyrosines in the activation loop of insulin were mutated to...

predict what would happen if the tyrosines in the activation loop of insulin were mutated to phenylalanine phenylalanines will likely be phosphorylated but insulin recptor will not be activated phenyalanines cannot be phosphorylated and insulin would not be activated phenylalanine will likely be phosphorylated and irs 1 will bind and be phosphorylated phenylalanine cannot be phosphorylated but irs 1 will bind and be phosphorylated

X and Y want to predict the outcome of the elections in their congressional district. X...

X and Y want to predict the outcome of the elections in their congressional district. X has been travelling to all neighborhoods of the district to ask people’s opinions about their favorite candidate. X has interview 2000 people and has found that 40% of them support the democrat candidate. Y has created a website where people can express their political opinions and he has advertised his website by putting some posters near his house. Y has found that 4000 people...

A psychic claims to be able to predict the outcome of coin flips before they happen....

A psychic claims to be able to predict the outcome of coin flips before they happen. Someone who guesses randomly will predict about half of coin flips correctly. In 100 flips, the psychic correctly predicts 57 flips. Do the results of this test indicate that the psychic does better than random guessing? The hypotheses are Ho:p=0.50 Ha:p>50 where p is the proportion of correct coin flip predictions by the psychic. 1. Give the test statistic for this problem. Group of...

28) Why do cells grow and become cancerous when p53 is mutated? A. The cancer cells...

28) Why do cells grow and become cancerous when p53 is mutated? A. The cancer cells stimulate blood vessel growth for nutrients and metastasis. B. p53 is a transcription factor which turns on a growth factor gene, thus stimulating mitosis. C. p53 is a transcription factor which turns on a gene for a growth-inhibitory protein. D. p53 is an oncogene which is integrated into genome from human papilloma virus. 29). If all humans are 99.9% same at DNA level, how...

Consider a “system with two lenses in tandem”. Suppose that you have an object that is...

Consider a “system with two lenses in tandem”. Suppose that you have an object that is located P1to the left of a lens with F1 focal length. Then suppose that you have a second lens with F2 focal length, and you place this lens D downstream of the first lens. Let us say that the final image of the optical system forms Q2 past the second lens. The two lenses are one after another, or in tandem. (a) Draw a...

Tyrosine is specified by two codons: UAU and UAC. Which of them is likely to be...

Tyrosine is specified by two codons: UAU and UAC. Which of them is likely to be found more frequently in thermophilic bacteria (those that live e.g. in volcanic hot springs)? Explain briefly.

A pentapeptide that contains histidine, two glycines, tryptophan, and alanine is incubated with the protease chymotrypsin....

A pentapeptide that contains histidine, two glycines, tryptophan, and alanine is incubated with the protease chymotrypsin. A dipeptide and a tripeptide result, and the dipeptide contains tryptophan while the tripeptide contains histidine and two glycines. Brief treatment with carboxypeptidase A yields free histidine. What is the sequence of the peptapeptide? Answer options: GGWAH GGHWA AWGGH GGHAW GWAGH

Eukaryotic protein x has one proline residue and two cysteine residues. The proline needs to be...

Eukaryotic protein x has one proline residue and two cysteine residues. The proline needs to be in the cis-configuration in the folding protein and a disulphide bond is formed between the cycteine residues in the folded protein. Discuss the folding of the protein in a solution with protein disulphide isomerases and peptidyl prolyl isomerases as well as without these enzymes. Make use of illustrations to show differences in the potential folding of protein x under different conditions.

Question