Becker's World of the Cell (9th Edition)
9th Edition
ISBN: 9780321934925
Author: Jeff Hardin, Gregory Paul Bertoni
Publisher: PEARSON
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Chapter 19, Problem 19.3CC
You are working in a lab to identify new alleles of a gene in the nematode Caenorhabditis elegans that encodes the protein β-catenin. Based on the
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The figure below shows the introns and exons found in gene X. The size of each exon and intron is shown as well. A study on this organism found that two
mature mRNA molecules are produced for this gene. One is 457 nucleotides in length, and the other is 439 nucleotides in length. Name the process responsible
for producing this variation. Also explain how these 457 and 439 nucleotide fragments were produced by referring to the information provided.
Hint: This organism produces a poly-A tail of 120 nucleotides.
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62
120
84
102
27
117
Gene X
E1
11
E2
12
ЕЗ
13
E4
Exon (E)
Intron (I)
The figure below shows the introns and exons found in gene X. The size of each exon and intron is shown as well. A study on this
organism found that two mature MRNA molecules are produced for this gene. One is 457 nucleotides in length, and the other is 439
nucleotides in length. Name the process responsible for producing this variation. Also explain how these 457 and 439 nucleotide
fragments were produced by referring to the information provided.
Hint: This organism produces a poly-A tail of 120 nucleotides.
99
62
120
84
102 27
117
Gene X
E1
в в
11
E2
12
E4
Exon (E)
Intron (1)
You are studying a mutation in mice, which acts dominantly. Mice that have only one copy of the allele carrying this mutation have a kinky tail phenotype. You identify the gene that the mutation affects and find that the codon that encodes the second amino acid in the predicted protein has been mutated to a stop codon. Would you characterize this mutation as a loss-of-function or a gain-of-function and what specific subtype (hypermorphic, antimorphic, etc. ) within these categories? Explain your reasoning.”
Chapter 19 Solutions
Becker's World of the Cell (9th Edition)
Ch. 19 - Suppose a tRNA has the anticodon 3-CGU-5. What two...Ch. 19 - Kanamycin is an antibiotic that binds to bacterial...Ch. 19 - You are working in a lab to identify new alleles...Ch. 19 - Suppose you are using GFP fusion proteins to study...Ch. 19 - Enzymes can undergo allosteric regulation or...Ch. 19 - Suppose you use molecular biology techniques to...Ch. 19 - Prob. 19.1PSCh. 19 - Tracking a Series of Mutations. The following...Ch. 19 - Prob. 19.3PSCh. 19 - Prob. 19.4PS
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- Consider a stretch of DNA (a hypothetical gene) that has the sequence 5’ ATG-CTA-TCA-TGG-TTC-TAA 3’ A) Transcribe and translate this gene using the genetic code table. Be sure to label the mRNA 3’ and 5’ ends. Write the amino acid sequence using 1 letter abbreviations. B) Now, our hypothetical gene has undergone a mutation. The mutant sequence is....3’ TAC-GAT-AGT-ACC-AAT-ATT 5’5’ ATG-CTA-TCA-TGG-TTA-TAA 3’ Transcribe and translate the mutant sequence. Be sure to label the mRNA 3’ and 5’ ends. Write the amino acid sequence using 1 letter abbreviations. C) Indicate the type of mutation (nonsense, missense, silent, or frame shift) present. D) How severe of a consequence will this mutation likely be in terms of protein function (none, mild, moderate or severe)? Why?arrow_forwardYou take DNA samples from a family with a history of the genetic disease spinal muscular atrophy, which results from many different mutations in the SMA gene. One mutation in the SMA gene is a 240-bp in-frame deletion mutation in the middle of an exon. Data from this family shows you that several individuals from the family have this mutation. What do you predict that you would find when comparing the mRNA and protein products of the mutated and unmutated SMA gene? Select all that apply. 1. The mRNA from the SMA is more stable than unmutated SMA mRNA. 2. The pre-mRNA from the SMA mutant is shorter than the unmutated SMA pre-mRNA. 3. The mature mRNA from the SMA mutant is longer than the unmutated SMA mRNA. 4. The protein from the mutated SMA is shorter than the unmutated SMA protein.arrow_forwardIn a disorder called gyrate atrophy, cells in the retina begin to degenerate in late adolescence, causing night blindness that progresses to total blindness. The cause is a mutation in the gene that encodes an enzyme, ornithine aminotransferase (OAT). Researchers sequenced the OAT gene for 5 patients with the following results: Patient A: A change in codon 209 of UAU to UAA Patient B: A change in codon 299 of UAC to UAG Patient C: A change in codon 426 of CGA to UGA Patient D: A two-nucleotide deletion at codons 64 and 65 that results in a UGA codon at position 79. Patient E: Exon 6, including 1071 nucleotides is entirely deleted. Which patient(s) have a frameshift mutation? How many amino acids is patient E missing? Which patient(s) will produce a shortened protein?arrow_forward
- You are interested in studying resistance to heavy metals and have selected the yeast Saccharomyces cerevisea to conduct your studies. You have recovered a deletion mutant that does not tolerate high concentrations of zinc (grows poorly in zinc containing media ) and have designated the mutant pgz-1 (for poor growth in zinc ). (a) What is the advantage to the type of mutant used in this work? What class of mutagen was likely use to generate pgz-1? ( b) Do you expect the PGZ gene to be expressed in your mutant? Explain.arrow_forwardDuchenne muscular dystrophy is caused by a mutation in a gene that comprises 2.5 million base pairs and specifies a protein called dystrophin. However, less than 1% of the gene actually encodes the amino acids in the dystrophin protein. On the basis of what you now know about gene structure and RNA processing in eukaryotic cells, provide a possible explanation for the large size of the dystrophin gene.arrow_forwardScientists are working to develop gene therapy to treat Batten disease, also known as Late Infantile Neuronal Ceroid Lipofuscinosis (LINCL). This fatal, autosomal recessive neurodegenerative disorder results from a mutation in the gene that codes for the enzyme TPP1 (Tripeptidyl peptidase 1). In the absence of this enzyme, a substance called ceroid lipofuscin accumulates in lysosomes in the brain, resulting in seizures, blindness, decline in cognitive function and motor skills, dementia, and death by the late teens or early 20’s. The TPP1 gene is 6695 bp in length. Think about the characteristics of Batten disease, and then suggest an approach to gene therapy that might be effective for this specific genetic disorder. You may assume that your research team is working in the U.S. and your research is funded by a grant from the National Institutes of Health (NIH). 1. Briefly outline a procedure that you could use to carry out the gene therapy for Batten disease.arrow_forward
- Huntington’s disease is a hereditary central nervous system disorder characterized by tandem repeats of the sequence 5'-CAG-3' in the gene that encodes a protein called huntingtin. The disease is progressive from generation to generation, meaning that in later generations the number of CAG repeats increases and the age of onset of symptoms decreases. Refer to Figure 21.4 and describe the sort of evidence supporting the generational increase in the number of CAG repeats.arrow_forwardThe figure shows the position of two of these mutations a and b. The nucleotides are altered in these 2 different swo-1 mutant alleles. Use the genetic table to describe any AA changes.Name the type of mutation and describe its effect on swo-1 mRNA and protein for each of the mutations. 3. The swo-1 a mutation (insertion between C and G). 4. The swo-1 b mutation (C-to-T mutation for indicated C). 5. The swo-1 a mutation leads to worms with more body wall muscle, whereas worms with the swo-1 b mutation are not able to move. Based on these phenotypes and the findings from questions 3 and 4, describe the role thewild-type version of this protein plays in muscle function.arrow_forwardYou may wish to consult the genetic code above to answer the following question. A mutation has changed a portion of a protein coding gene that encodes a messenger RNA sequence. The original messenger RNA sequence is 5-AUGCCCAGAGCU-3' Which mutation is a nonsynonymous (missense) mutation that changes a single amino acid in the encoded protein? O 5-AUGCCCAGGGCC-3' O 5'-AUGCCCUGAGCU-3' O 5'-AUGCCCACAGCU-3 5'-AUGCCCCAGAGCU-3arrow_forward
- You 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.arrow_forwardThe length of a particular gene in human DNA, measured from the start site for transcription to the end of the protein-coding region, is 10,000 nucleotides, whereas the length of the mRNA produced from this gene is 4000 nucleotides. What is the most likely reason for this difference?arrow_forwardHere is a eukaryotic gene. The numbers given are base pairs of exon and intron. How long in bases will the pre mRNA transcript be? Explain briefly. What is the maximum number of amino acids that could make up the protein product from the final mRNA? Explain briefly.arrow_forward
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Mitochondrial mutations; Author: Useful Genetics;https://www.youtube.com/watch?v=GvgXe-3RJeU;License: CC-BY