Genetics Q8 8. In the rock pocket mouse's Mc1r gene, there are five mutations. What are these? Identifywhich ones are substitutions, insertions or deletions.

Research suggests there might be some ambiguity regarding the number and specific mutations in rock…

Answered: 8. In the rock pocket mouse's Mc1r…

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter11: Genome Alterations: Mutation And Epigenetics

Section: Chapter Questions

Problem 9QP: Define and compare the following types of nucleotide substitutions. Which is likely to cause the...

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If the coding region of a gene (the exons) contains 2,100 base pairs of DNA, would a missense mutation cause a protein to be shorter, longer, or the same length as the normal 700 amino acid proteins? What would be the effect of a nonsense mutation? A sense mutation?
What are deletion mutations? Also plzz mention its types Quickkkkk
Describe the mutation that occurs in the following examples (be specific, if possible): BOAT to BAT SOAP to SOUP PAY to PLAY GCTCT to GCACT TGCCC to TACCC CATGC to GATGC TATATA to TACATA
4) The fact that splicing is a strategy to optimize the use of the genome in eukaryotes is evidenced in C. elegans, which with 20,000 genes can synthesize more than 20,000 proteins. True or false 7) The mutation in the myostatin protein that results in mice with hypertrophied muscles results from a premature stop codon that results in a truncated (shorter than necessary) protein that loses its function of stopping cell division of muscle cells. What post-transcriptional quality control mechanisms fail here? (two apply) a) polyadenylation b) NMD c) splicing d) capping e) methylation 10) The nuclear transplant experiment results in: a) KO or knockout b) transgenic organisms c) RNAi (interference) d) animal cloning
An investigator was interested in studying UAG nonsense suppressor mutations in bacteria. In one speciesof bacteria, she was able to select two different mutants of this type, one in a tRNATyr gene and the otherin a tRNAGln gene, but in a second species, she wasnot able to obtain any such nonsense suppressor mutations, even after very extensive effort. What couldexplain the difference between the two species?
1. Using the data available describe the phenotype that you observe when each of these three genes is knocked down using RNAi. Remember to compare the worms on control RNAi plates with worms on each of the RNAi knockdown plates. In each case state how do these phenotypes relate to the function of the gene. （gene name for F27C1.8 is dpy-5，for T19E7.2 is skn-1） 2. Describe further experiments that you could do that would confirm your findings.
Do you think each of the following types of mutationswould have very severe effects, mild effects, or no effectat all?a. Nonsense mutations occurring in the sequences encoding amino acids near the N terminus of the proteinb. Nonsense mutations occurring in the sequences encoding amino acids near the C terminus of the proteinc. Frameshift mutations occurring in the sequences encoding amino acids near the N terminus of the protein d. Frameshift mutations occurring in the sequencesencoding amino acids near the C terminus of theproteine. Silent mutationsf. Conservative missense mutationsg. Nonconservative missense mutations affecting theactive site of the proteinh. Nonconservative missense mutations not in the active site of the protein
A reversion is a mutation that returns a mutant codon back to acodon that gives a wild-type phenotype. At the DNA level, this typeof mutation can be an exact reversion or an equivalent reversion. An equivalent reversion produces a protein that is equivalent to thewild-type protein in structure and function. This outcome canoccur in two ways. In some cases, the reversion produces thewild-type amino acid (in this case, glutamic acid), but it uses adifferent codon than the wild-type gene. Alternatively, an equivalentreversion may substitute an amino acid structurally similarto the wild-type amino acid. In our example, an equivalent reversionhas changed valine to an aspartic acid. Because aspartic andglutamic acids are structurally similar—they are acidic aminoacids—this type of reversion can restore wild-type structure andfunction.Here is the question: The template strand within the codingsequence of a gene has the following sequence:3′–TACCCCTTCGACCCCGGA–5′This template produces the…
Name three different types of loss of function mutations and in each case explain how the mutation exerts a loss of function effect on a gene
Define FOUR (4) types of point mutations within coding sequences
The amino acid sequence of part of a protein has beendetermined:N . . . Gly Ala Pro Arg Lys . . . CA mutation has been induced in the gene encodingthis protein using the mutagen proflavin. The resultingutant protein can be purified and its amino acidsequence determined. The amino acid sequence of themutant protein is exactly the same as the amino acidsequence of the wild-type protein from the N terminus of the protein to the glycine in the preceding sequence. Starting with this glycine, the sequence ofamino acids is changed to the following:N . . . Gly His Gln Gly Lys . . . CUsing the amino acid sequences, one can determinethe sequence of 14 nucleotides from the wild-typegene encoding this protein. What is this sequence?
a. Some antibiotics, such as rifampin, interfere with the function of RNA polymerase. What biological process is rifampin disrupting? b. Some antibiotic-resistant M. tuberculosis bacteria have a single point mutation (CàT) in the rpoB gene that causes an amino acid change from serine (a polar amino acid) to leucine (a non-polar amino acid). What type of mutation is this? Do you expect this to have no effect, a small effect, or a large effect on the polypeptide produced? Explain your reasoning. c. The rpoB gene encodes a subunit of the bacterial RNA polymerase protein. The point mutation described in Question 2 causes a change in protein folding, which leads to the inability of the rifampin antibiotic to bind to the RNA polymerase. Which level(s) of protein structure is/are affected by this change?

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