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You are examining the processing of rRNA in E. Coli using a Northern blot. Normally, a 30S rRNA transcript is transcribed and then processed (cleaved) into 23S, 16S, and 5S mature rRNAs. You suspect the gene RPO7 is involved, so you make a mutant strain of bacteria and compare it to a Wild-type (Wt) strain. You run RNA extracts from the two strains on a Northern blot and probe it with a radioactive probe that binds to all rRNA. You get the following results.
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- You are studying the tryptophan synthetase gene that Yanofsky also examined to determine the relationship between the nucleotide sequence and the amino acid sequence of the gene. Yanofsky found a large number of mutations that affected the tryptophan synthetase gene. A) If you took this mutant E. Coli line (that has an Arginine at this location) and exposed it to a mutagen that could potentially change bases, what are the second mutations you would most likely discover that would restore the activity of the tryptophan synthetase gene and where would it be located? B) Most of the mutations that Yanofsky recovered were missense mutations. However, Yanofsky also recovered a nonsense mutation that changed amino acid number 15 into a stop codon. This codon normally encodes Lysine. Does the recovery of this mutation support the hypothesis that this Lysine residue is critical in the function of the tryptophan synthetase protein?. You are interested in a eukaryotic protein involved in immunity, and you are attempting to express this protein in E. coli in order to produce large amounts of the protein. You have identified the gene and place a copy of the gene on a plasmid in E. coli next to a bacterial promoter sequence. You determine that lots of mRNA is made from your gene in your E. coli system, but the protein produced is larger and doesn't have the same properties as the eukaryotic protein you expected. What mistake have you made and how can you fix it?Researchers are manipulating the gene cxx2 for their experiments, and they have inserted a smallnumber of base pairs randomly somewhere into the gene. They isolate several versions (with differentinsertions) of this modified gene and carry out an RT-PCR using a primer that recognizes thetranscriptional start site area (eg. from +1 to +20), and a primer that binds to the polyA tail.For the second modified gene sample, they observe that the mature mRNA is now several basepairs longer, however splicing has not been affected. They examine the protein and identify thatit has significant changes to its amino acid sequence, altering its length. Which of the letteredarrowheads indicates the location where this insertion could be? (There could be one answer orseveral. Give all answers that apply)
- Starting with a sample of RNA that contains the mRNA for theβ-globin gene, explain how you could create many copies of theβ-globin cDNA using reverse transcriptase PCR.Now that you understand how the CRISPR-Cas9 system works, think back to the experiments discussed in the introduction to this chapter, in which researchers used CRISPR-Cas9 genome editing to treat mice with Duchenne muscular dystrophy. Why did the researchers choose to cut out the entire exon 23 in the mice with the disorder? Why not replace the specific mutation using a donor piece of DNA and homologous recombination? Propose some possible explanations.Analyzing Cloned Sequences A base change (A to T) is the mutational event that created the mutant sickle cell anemia allele of beta globin. This mutation destroys an MstII restriction site normally present in the beta globin gene. This difference between the normal allele and the mutant allele can be detected with Southern blotting. Using a labeled beta globin gene as a probe, what differences would you expect to see for a Southern blot of the normal beta globin gene and the mutant sickle cell gene?
- Early gene-cloning experiments involved insertion at one restriction site in the vector; for example, the insert would have an EcoRI site at each end, and the vector would be opened at an EcoRI site prior to ligation. Under what circumstances would asymmetric cloning be desirable, with the insert having a different restriction site at each endIf I clone a complete eukaryotic gene, including the eukaryotic promoter region, ligate it into a plasmid, and transform it into E. coli, will I be able use the transformed E. coli to make the corresponding protein? Explain why, or why not? If you decide to do this, what would your cloning strategy be?If you wanted to express a library of human proteins in yeast, there are several good reasons why it would be better to use a cDNA library instead of a genomic library from humans. Which one of the following options is not such a reason? a. yeast may not initiate transcription or splicing of a human gene at the correct locations b. some genes will have very high representation (many plasmids contain the gene), while others will have very low representation (few or no plasmids contain the gene) in the cDNA library c. most genomic library clones would be useless, because only ~1.5% of the human genome actually encodes proteins d. a cDNA library can contain multiple splice variants, which are common for human genes e. introns are often very large in the human genome, making it impossible in many cases to contain a genomic version of an entire gene in a single plasmid
- In generating mutations in a bacterial gene involved in antibiotic resistance, a number of point mutations are isolated that render the bacteria sensitive to the antibiotic. You would like to sequence the gene in order to characterize the mutations, but unfortunately, your lab partner just finished the last of the lab's supply of DNA polymerase. The only things at your disposal are materials for performing a western blot, allowing you to visualize the protein encoded by the gene. How would you identify which mutations are likely to be the result of a missense mutation, which are likely to be the result of a nonsense mutation, and which are likely to be the result of a frameshift mutation?Design a site directed mutagenesis experiment to convert the wild type GFP sequence into the S65T mutant. You must include the sequence of the primers, and outline of the PCR conditions you would use, and the protocols for the mutagenesis and transformation of bacteria with your plasmid containing the mutation.Why aren’t primary rRNA transcripts present in wild-type E. coli?