While prokaryotic and eukaryotic transcription processes are quite similar, there are some key differences. One significant difference is that prokaryotic transcripts can contain multiple genes, which will then transition as a single RNA strand to the ribosome. This is referred to as a polycistronic transcript. Eukaryotes have only one gene per transcript.

Both prokaryotes and eukaryotes use promoters. Prokaryotes do not have nuclei, though transcription and translation can occur simultaneously and in close proximity in these cells.

The correct answer is operator. In most operons, repressors bind operators to prevent transcription of downstream genes.

Promoters are sequences of DNA upstream of genes that usually promote transcription by recruiting polymerases and other transcription factors. Enhancers are distant DNA sequences that promote transcription, whereas exons are the coding segments of a gene.

The lack of a nuclear membrane in prokaryotes has the advantage of allowing the cell to translate RNA as it is transcribed from DNA. This means that even before the full RNA is produced, the protein coded by that RNA can start being made. Eukaryotes produce RNA inside the nucleus, so it must first be fully transcribed and undergo modifications before it can be moved to the cytoplasm, where translation occurs.

RNA polymerase does not interact with the Shine-Delgarno sequence. The Shine-Delgarno sequence is present on some prokaryotic mRNAs and serves as a ribosomal binding site for the initiation of translation. RNA polymerase is only involved in transcription and will bind to DNA, not RNA.

The other answers are all true and unique to prokaryotic transcription. Eukaryotic transcription is much more tightly regulated by transcription factors and DNA packaging (chromatin), and is confined to the nucleus.

There is only one codon that signals the start of translation: AUG. This codon codes for the amino acid methionine so this amino acid will also be at the N-terminus of all proteins, however it may be removed and/or modified later.

The three types of RNA discussed are messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). mRNA forms during transcription when RNA polymerase synthesizes RNA from the DNA template. Post-transcriptional modification is required for the mRNA to mature and exit the nucleus. Once in the cytoplasm, the mRNA will bind to a ribosome composed of rRNA and proteins. The ribosome will then recruit tRNA molecules to the complex in order to synthesize the protein product. Each amino acid binds to a specific kind of tRNA. tRNA brings the amino acids to the growing end of the newly forming polypeptide at the ribosome by binding to the codon of the mRNA.

Quaternary protein structure is distinguished by the fact that several polypeptide chains come together to make a functional protein. This is different than the first three levels of protein structure, which only involve one polypeptide chain. Quaternary structure is held together primarily by hydrophobic interactions between the polypeptide chains (ionic and/or hydrogen bonding is often seen as well). Each polypeptide chain forms a subunit of the protein.

There are a number of ways that scientists study protein folding and structure. They include the following processes: mutation studies, x-ray crystallography, and spectroscopy. Mutation studies compare the folding patterns of wild type proteins and those with targeted point mutations. X-ray crystallography is a form of high-resolution microscopy that uses x-rays to study the atomic structure of protein crystals through diffraction patterns. Last, a number of spectroscopy methods are employed to study protein folding by comparing unfolded, folded, and partially folded proteins.

The protein quaternary structure is the highest level of protein architecture and refers to the arrangement of protein subunits and their interactions with one another. There is a range in the complexity in the quaternary structure of proteins from dimers, such as DNA polymerase, to tetramers, such as hemoglobin. These structures are always composed of more than one protein subunit.

The tertiary structure of protein folding has a polypeptide chain backbone and a number of protein secondary structures: alpha helices and beta-pleated sheets. The tertiary structure is three-dimensional. The protein folding that causes the formation of the tertiary structure is influenced by hydrophobic interactions, disulfide bridges, hydrogen bonds, and salt bridges that create hydrophobic and hydrophilic regions.