For this lac mutant in an E. coli strain, indicate whether B-galactosidase and permease would be expressed in the absence or presence of lactose in the cell. Copy and fill out the table or similar. Also, explain the most important mutants or events that determine gene expression in this cell. lacı* lacP+ lacOʻlacz+ lacY+ Lactose present B-galactosidase present/absent Lactose absent B-galactosidase present/absent permease permease present/absent present/absent
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- For each of the E. coli strains that follow, indicate theeffect of the genotype on the expression of the trpEand trpC genes in the presence or absence of tryptophan. [In the wild type (R+ P+ o+ att+ trpE+ trpC+),trpC and trpE are fully repressed in the presence oftryptophan and are fully expressed in the absence oftryptophan.]R = repressor gene; Rnproduct cannot bind tryptophan; R− product cannot bind operatoro = operator for the trp operon; o− cannot bind repressoratt = attenuator; att− is a deletion of the attenuatorP = promoter; P− is a deletion of the trp operonpromotertrpE− and trpC− are null (loss-of-function) mutationsa. R+ P− o+ att+ trpE+ trpC+b. R− P+ o+ att+ trpE+ trpC+c. RnP+ o+ att+ trpE+ trpC+d. R− P+ o+ att− trpE+ trpC+e. R+ P+ o− att+ trpE+ trpC−/R− P+ o+ att+trpE− trpC+f. R+ P− o+ att+ trpE+ trpC−/R− P+ o+ att+trpE− trpC+g. R+ P+ o− att− trpE+ trpC−/R− P+ o− att+trpE− trpC+The lac genotypes are as shown below: P+OcZ-Y+A+// P¯O+Z+Y+A+ (i) The lac operon consists of three structural genes, lacZ, lacY and lacA. Which structural genes are involved in lactose metabolism? Explain. (ii) Draw and explain how lactose repress the gene expression in lac IS/I- heterozygote. (iii) What is the function of the promoter in the bacterial operon?Direct mutagenesis of Ca2+ ATPase gene resulted in the replacement of two amino acid residues - Asn111 and Asn114 to Ala. These substitutions led to the reduction in Ca2+ transport activity by 10% and 50%, respectively. On the other hand, directed mutagenesis that resulted in the alteration of four Glu residues in the lumenal loop of this transport protein to Ala, did not affect the Ca2+ transport. Provide the possible explanation for the observed differences in the Ca2+ transport activity between the protein with Asn->Ala substitution and the protein with Glu->Ala substitution.
- I have this strain of e coli. Is P+ o+ Z+ Y+ / I- P+ oC Z- Y+ Will beta-galactosidase and permease be expressed? If they are will they be inducible or constitutive?Searching the yeast Saccharomyces cerevisiae genome, researchers found approximately 4,000 DNA sites with a sequence which could potentially bind the yeast transcription factor GAL4. GAL4 activates the transcription of galactose genes. Yet there are only 10 GAL4-binding sites which control the genes necessary for galactose metabolism. The GAL4 binding sequence is CGGAT#AGAAGC*GCCG, where # is T, C or G, and * is C or T. In one chromatin immunoprecipitation experiment (ChIP), yeast growing on galactose were lysed, and subjected to cross-linking reagents which cross-linked transcription factors and activators to DNA. Next the DNA was sheared into small fragments, and antibodies to GAL4 were added. These antibodies coprecipitated the GAL4 and the DNA it was cross-linked to. The cross-linking was then chemically reversed, and the DNA was isolated, cloned into a library of plasmids and sequenced. Results showed that only 10 different DNA sequences had GAL4 bound. Since the…I-cell disease is a classic example of an inherited human defect in protein targeting that affects an entire class of proteins: the soluble enzymes of the lysosome. What is the molecular defect in I-cell disease? Why does it affect the tar- geting of an entire class of proteins? What other types of mutations might produce the same phenotype?
- During periods of sustained demand and in the presence of sufficient nutrients, muscle cells can increase in size. When the size of muscle cells increases, they will often develop additional nuclei in their intracellular environment. Which of the following is the most likely explanation for the expression of additional nu- clei in growing muscle cells? A B с D Nutrients entering the cells will be digested and recycled more quickly by the additional nuclei to better support the subcellular components in the cell as its size increases. The ATP molecules that are produced in the additional nuclei will be able to better sup- port the increased energetic demands on the muscle cell as its size increases. The addition of more nuclei to the cell will allow more genetic information to be stored in the cell and allow the cell to produce additional types of proteins as its size increases. Additional nuclei allow subcellular components to continue to be sufficiently expressed and transferred…If lactose is present in a cell with the following genotype, will functional Beta – galactosidase and/or permease be made? LacIs, LacP+, LacOc, LacZ+, LacY- / LacI+, LacP+, LacO+, LacZ-, LacY+ Group of answer choices Both genes will make functional protein. Only Beta – galactosidase will be functional. Only permease will be functional. No functional proteins will be made.A particular type of anemia in humans, called b-thalassemia,results from a severe reduction or absence of the normal b-globinchain of hemoglobin. However, the g@globin chain, normally onlyexpressed during fetal development, can functionally substitutefor b-globin. A variety of studies have explored the use of thenucleoside 5-azacytidine for the expression of g-globin in adultpatients with b-thalassemia.(a) How might 5-azacytidine lead to expression of g-globin inadult patients?(b) Explain why this drug may also have some adverse side effects.
- The codon change (Gly-12 to Val-12) in human rasH that convertsit to oncogenic rasH has been associated with many types ofcancers. For this reason, researchers would like to develop drugs toinhibit oncogenic rasH. Based on your understanding of the Rasprotein, what types of drugs might you develop? In other words,what would be the structure of the drugs, and how would theyinhibit Ras protein? How would you test the efficacy of the drugs?What might be some side effects?In this chapter you were introduced to nonsense suppressor mutations in tRNA genes. However, suppressormutations also occur in protein-coding genes. Using thetertiary structure of the β subunit of hemoglobin shownin Figure 9-3(c), explain in structural terms how a mutation could cause the loss of globin protein function. Nowexplain how a mutation at a second site in the same protein could suppress this mutation and lead to a normalor near-normal protein.Wilms tumor 1, or nephroblastoma, is caused by mutations in the WT1 gene, which encodes a transcription factor. You have identified a novel variant in WT1: Arg422Pro. You have control cells and cells that have been engineered to carry the homozygous WT1 p.Arg422Pro mutation. You want to assess effects of this mutation on a variety of endpoints. For each endpoint listed below, choose the one technique is best suited to answer the question. Choose from: array CGH, qRT-PCR, qPCR, RNA-seq, FISH, in situ hybridization, western blot, immunostaining, WT1 ChIP-seq, WT1 ChIP-PCR, ATAC-seq, 3C Endpoint Technique? WT1 protein amount (quantitative) Western blot WT1 protein binding to all enhancers, genome-wide Chip-seq WT1 mRNA amount (quantitative) WT1 protein subcellular localization Quantitative assessment of all mRNAs in these cells (genome-wide) RNAseq Chromatin interactions between a specific WT1 chromatin binding site (identified above)…