Antibiotics are able to inhibit protein synthesis in prokaryotes in a number of ways. The specific method of inhibition depends on the antibiotic that is used. Examples of the antibiotics that target translation are rifamycin, linezolid, and tetracyclines. Rifamycin inhibits RNA polymerase and the resulting synthesis of mRNA. Linezolid blocks the formation of the translation initiation complex. Tetracyclines obstruct the aminoacyl “A” site of ribosomes. Inhibiting translation is an effective way to kill bacteria and treat bacterial infections. Antibiotics specifically target prokaryotic cells, ensuring no harm to the host eukaryotic cells. 

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 involved in Translation are messenger RNA, transfer RNA, and ribosomal RNA.

Many amino acids have multiple three-nucleotide sequences that correspond with them. If a sequence that codes for leucine (UUA) is mutated by only one letter (to UUG), then it will still form a functional protein, since the mutated sequence also codes for leucine. Redundancy allows occasional mutations to occur without corrupting the amino acid sequence.

DNA polymerase is not involved in the transcription of mRNA to amino acids.

A single three-nucleotide sequence can only code for a single amino acid, although many amino acids can be coded for by multiple nucleotide sequences (redundancy).

Each tRNA contains the anticodon for a specific mRNA codon and carries the amino acid corresponding to that codon to ribosomes during translation. mRNA is produced by transcription from DNA, and ribosomes translate it into proteins. Multiple codons can code for a single amino acid, and so there can be several tRNA anticodons that could be used for a single amino acid.

mRNA, tRNA, and rRNA all play a key role in the synthesis of proteins. tRNA (transfer RNA) is responsible for gathering amino acids in the cytosol and bringing them to the ribosomes when translation is taking place. mRNA (messenger RNA) is the template for translation. rRNA (ribosomal RNA) is a structural element of the ribosomes.

An anticodon is the three-base sequence, paired with a specific amino acid, that a tRNA molecule brings to the corresponding codon of the mRNA during translation. The anticodon sequence is complementary to the mRNA, using base pairs in the anti-parallel direction. tRNA is read 3'-to-5', so the sequence would be 3'-UUG-5'. Keep in mind that adenine binds to uracil in RNA.

Codon:      5'-AAC-3'

Anticodon: 3'-UUG-5'

Anticodons are found on molecules of tRNA. Their function is to base pair with the codon on a strand of mRNA during translation. This action ensures that the correct amino acid will be added to the growing polypeptide chain. A tRNA molecule will enter the ribosome bound to an amino acid. The anticodon sequence will bind to the codon of the mRNA, allowing the tRNA to release the attached amino acid. This amino acid is then added to the peptide chain by the ribosome.

tRNA is a special type of RNA that has the function of forming bonds with amino acids and bringing them to ribosomes to complete translation. tRNA carries anticodons, allowing it to bind to mRNA in the active site of a ribosome. It can then transfer its amino acid residue to the ribosome, where it is incorporated into the growing polypeptide chain. The tRNA molecule is the released from the ribosome and recycled.

rRNA forms part of the ribosome structure and mRNA brings information from the nucleus to the cytoplasm. Transcription is the process of making an RNA transcript from a DNA template, and is performed by an RNA polymerase.

Amino acid sequence is determined by the sequence of codons on mRNA. tRNA is responsible for bringing new amino acids to the ribosome. Interactions between the codons on mRNA and the anticodons on tRNA are what allow the formation of the appropriate peptide bonds.

Chaperones are later used to facilitate the development of protein structure, but are not involved in checking protein sequence.