The question informs us that the mutational defect in the gene involves the enzyme's ability to load copper onto apoceruloplasmin. Healthy individuals are able to load copper to apoceruloplasmin, creating serum-soluble ceruloplasmin. With this process disrupted in an individual with Wilson's Disease, we would expect that less ceruloplasmin would be produced because copper could not be transported. We would expect to see reduced serum levels of the complete protein, and high levels of copper building up in hepatocytes and circulatory serum.

The addition of a number of nucleotides that is not a multiple of three shifts the reading frame of the codons in the gene. One base pair was inserted early in the strand, thus shifting the codon reading frame +1 to the right.

Missense and nonsense mutations imply base pair substitutions, which did not occur in the diagram. Similarly, nothing was duplicated, and repeat expansion would require multiple repetitions of a short DNA sequence.

This question requires the knowledge that a dominant negative is expected to work in the same direction as a genetic mutant; it is a loss-of-function of the gene, by expressing a version of the gene that outcompetes the actual gene but cannot perform the proper biological process. Because we are assuming the dominant negative works perfectly, it should act just like the mutant and reduce cell number by 50%, giving us 50,000 cells. 

Transcription factors can be activated or deactivated by any number of processes occurring within the cell and nucleus, and this it not limited to phosphatases (which remove phosphate groups from proteins). All of the other answers accurately describe possible activity and function of transcription factors.

Only the first statement in this question is false. Transcription factors typically (in fact, almost always) bind upstream of the gene to enhancer or promoter regions, and are rarely found interacting with the gene's coding region itself. 

Of the three choices, the only element commonly found in a eukaryotic promoter is a TATA element. This is the site where TBP (TATA binding protein) binds and begins to recruit other transcriptional machinery.

The Shine-Delgarno sequence is commonly found on prokaryotic mRNA and serves as a ribosomal binding site. Because promoters are regions of DNA, both option I and II do not really apply.

The binding of RNA polymerase and transcription factors is tightly modulated by promoter elements. If affinity was increased compared to a wild-type sequence, we would expect that RNA polymerase would bind more easily to the sequence and produce more mRNA. Nothing about the nature of this mRNA is altered (since the coding sequences are unchanged); there is simply more of it, which would mean overexpression of the protein for which it codes.

The correct answer is promoter. The promoter is directly upstream of the start of transcription for a given gene. It is the site of transcription factor and RNA polymerase binding, and interacts with distant enhancers to regulate transcription. 

DNA polymerase is a crucial factor required for replication of DNA, but is not a component utilized in the process of transcription. The core promoter sequence, activators, and transcription factors are all needed in order for RNA polymerase to begin the process. 

Most proteins that will be embedded in the plasma membrane are translated on ribosomes located in the rough endoplasmic reticulum. There are specific mechanisms and proteins that help insert the proteins into the membrane while they are being translated. Free-floating proteins are more likely to be translated in the cytosol. The nucleus and the Golgi do not have ribosomes used for translation, though the Golgi can play an important role in transporting proteins from the rough endoplasmic reticulum to the membrane.