Protein synthesis can be divided into two main parts: transcription, which occurs in the nucleus, and translation,

which occurs at the ribosomes. However, because prokaryotes dont have a nucleus, transcription and translation both occur in the cytoplasm for them. Transcription involves the synthesis of an RNA transcript using the cell's DNA as a template, leading to mRNA. Translation is the whole process by which the base sequence of an mRNA is used to order and to join the amino acids in a protein. The three types of RNA participate in this essential protein-synthesizing pathway in all cells. First, mRNA migrates from the nucleus to the cytoplasm. During this step, mRNA goes through different types of maturation in which non-coding sequences are eliminated. The coding mRNA sequence can be described as a unit of three nucleotides called a codon. Next, translation starts at the 5 end of mRNA. In the cytoplasm, protein synthesis is initiated by the AUG codon on mRNA, which codes for methionine. The initial methionine is called the N-terminus. The start codon is positioned in the P (peptidyl) site of the ribosome, and is paired with the initiator tRNA (fMet-tRNA or Met-tRNA). The union of mRNA, initiator tRNA, and a ribosomal subunit form a complex; these components are all brought together by initiation factors. This complex is able to be produced because GTP molecules provide energy from their phosphate groups. After the initiation process, the initiator tRNA sits in the P site, which carries the growing polypeptide chain, and the vacant A site becomes available for the next tRNA. The A site holds the tRNA carrying the next amino acid to be added to the chain. Chain elongation begins with the binding of the complementary anticodon on the tRNA, which recognizes the next codon in the mRNA, to the A site of the ribosome. This is catalyzed by the EF-Tu transcription factor and requires the hydrolysis of a GTP. Once the tRNA binds to the A site of the ribosome, the polypeptide chain is moved from the tRNA in the P site to the amino acid attached to the tRNA in the A site. Then, peptidyl transferase, an enzyme in the 50s ribosomal subunit, catalyzes the formation of this new peptide bond between the amino acids. The ribosome then translocates to the next codon. This process is promoted by elongation factor G (EF-G), and requires another GTP. This places the empty tRNA molecule in the E site of the ribosome, and moves the tRNA containing the growing polypeptide chain in the P site. The next codon in the mRNA chain is positioned in the A site. The empty tRNA in the E site then leaves the ribosome and a cycle of chain elongation is completed. Termination begins when a stop codon (UGA, UAA, or UAG) appears in the A site. Since there is no anticodon on tRNA corresponding the stop codon, a release factor binds in the A site. The binding of the release factor causes the polypeptide chain to be cleaved from the tRNA by hydrolysis, completing the synthesis of the polypeptide. Finally, the two ribosomal subunits and the mRNA dissociate from each other.