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.

A tRNA that is attached to one amino acid will enter the ribosomal complex at the A site. It will then receive the growing polypeptide chain from the previous tRNA and move into the P site. Once handing off the chain, the tRNA that no longer has an amino acid will exit the ribosome at the E site.

The peptide chain is always anchored in the P site, where peptide bond synthesis occurs.

The genetic code is unambiguous, meaning that each given codon will always code for the same amino acid. An amino acid, however, can be coded for by multiple codons, making the genetic code degenerative in nature. Once a stop codon is reached during translation, the ribosome stops making the protein.

All of the post-transcriptional modifications listed occur in the nucleus. Each is important in the process of turning pre-mRNA into mature mRNA that can successfully exit the nucleus and enter into translation. These modifications allow for the appropriate recognition by ribosomes and serve to enhance the stability of the mRNA molecule.

The 5' guanosine cap is added to one end of the RNA strand, and a poly-A tail is added to the other. These modifications serve to help with ribosome recognition and prevent degradation. Spicing involves the removal of non-coding introns from the RNA transcript, allowing for translation of the proper sequence.

Ubiquitination is the only option in which the modification to the protein does not include the binding of a lipid group to a protein. Rather, it is the addition of another peptide to the existing protein.

Polyadenylation results in a long chain of adenosine monophosphate residues being added to the 3' end of a pre-mRNA as transcription is terminating. The poly-A tail provides stability to the mRNA molecule as it is transported through the cell to its ultimate location. Without this modification, the shorter mRNA would be degraded by enzymes within the cytoplasm. The other functions listed as answers are in no part dependent on the poly-A tail.