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. 

Conjugation of ubiquitin molecules to a protein activates the ubiquitin proteasome system, which is required by cells to break down proteins into their component amino acid residues to be reallocated in protein building as necessary. While the other modifications may contribute to some degradation pathway, ubiquitin is classically considered a marker of protein destruction via the proteasome system. 

Polyadenylation is the process in which a "Poly-a tail," or a tail of adenine bases, is added to the 3' end of an mRNA. The other processes listed do not carry out this function.

Epigenetics are changes to the genome that result in phenotypic variation that have nothing to do with changes in the actual DNA sequence. All listed answers occur independently of DNA sequence, except for "different exon sequences," which is the actual sequence of an exon. This referces to alternative splicing, an is not related to the modification of DNA or histones.

Methylation and acetylation of histones occurs on lysine residues, thereby decreasing or increasing gene expression, respectively. Methylation increases the affinity for histones and DNA, where acetylation decreases the affinity for histones and DNA. Gene expression is in part controlled by modification of histone proteins, rather non-histone chromosomal proteins. 

The correct answer is an increase in gene expression. Histone acetylation removes positive charges on the histones, reducing the affinity of DNA for histones. Remember that DNA is negatively charged due to the phosphate groups on its backbone. DNA and histones are attracted to each other because histones are positively charged due to being rich in basic amino acid residues. Acetylation relaxes the tightly bound DNA allowing transcription factors to bind promoter regions. DNA deacetylation and methylation supress gene transcription by making DNA and histones associate more tightly together, decreasing the ability of transcription factors and/or RNA polymerase to bind the DNA. Histone modifications such as acetylation, deacetylation, and methylation do not directly affect the amount of DNA. If a histone is acetylated on a part of the DNA which codes for the genes for ribosome production, then an increase in ribosomal production and assembly could occur, but genes coding for ribosomes are greatly outnumbered by other genes, and thus, this is not the usual result of acetylating histones.