TRANSLATION This is the conversion of the information of mRNA into proteins; messenger RNA produced by transcription is decoded by the

ribosome to produce a specific amino acid chain, or polypeptide, that will later fold into an active protein. Occurs in the ribosomes which exist as dissociate subunit in the cytoplasm and thus have to be assembled together before translation can take place. The ribosome facilitates decoding by inducing the binding of tRNAs with complementary anticodon sequences to that of the mRNA. The tRNAs carry specific amino acids that are chained together into a polypeptide as the mRNA passes through. It involves several steps; Activation In activation, the correct amino acid is covalently bonded to the correct transfer RNA (tRNA). The amino acid is joined by its carboxyl group to the 3' OH of the tRNA by a peptide bond. When the tRNA has an amino acid linked to it, it is termed "charged". Initiation Initiation of translation usually involves the interaction of certain key proteins with a special tag bound to the 5' cap. The protein factors bind the small ribosomal subunit (40S), and these initiation factors hold the mRNA in place. The eukaryotic Initiation Factor 3 (eIF3) is associated with the small ribosomal subunit, and plays a role in keeping the large ribosomal subunit from prematurely binding. eIF3 also interacts with the eIF4F complex which consists of three other initiation factors: eIF4A, eIF4E and eIF4G. eIF4G is a scaffolding protein which directly associates with both eIF3 and the other two components. eIF4E is the cap-binding protein. It is the rate-limiting step of cap-dependent initiation, and is often cleaved from the complex by some viral proteases to limit the cell's ability to translate its own transcripts.

Elongation With the formation of the complex containing fMet-tRNA in the peptidyl site, an aminoacyl tRNA with the complementary anticodon sequence can bind to the mRNA passing through the acceptor site. This binding is aided by elongation factors that are dependent upon the energy from the hydrolysis of GTP. Elongation factors go through a cycle to regenerate GTP after its hydrolysis.

Now, with tRNA bearing a chain of amino acids in the ribosome p site and tRNA containing a single amino acid in the ribosome A site, the addition of a link to the chain can be made. This addition occurs through the formation of a peptide bond, the nitrogen-carbon bond that forms between amino acid subunits to form a polypeptide chain. This bond is catalyzed by the enzyme peptidyl transferase. The peptide bond occurs between the carboxyl group on the lowest link in the peptide chain located at the p site and the amine group on the amino acid in the A group. As a result, the peptide chain shifts over to the A site, with the original amino acid on the A site as the lowest link in the chain. The tRNA in the A site becomes peptidyl RNA, and shifts over to the P site. Meanwhile, the ribosome engages in a process called translocation: spurred by elongation factors, the ribosome moves three nucleotides in the 3' prime direction along the mRNA. In other words, the ribosome moves so that a new mRNA codon is accessible in the A site. Termination Translation ends when one of three stop codons, UAA, UAG, or UGA, enters the A site of the ribosome. There are no aminoacyl tRNA molecules that recognize these sequences. Instead, release factors bind to the P site, catalyzing the release of the completed polypeptide chain and separating the ribosome into its original small and large subunits. POSTTRANSLATIONAL MODIFICATION This is a process which involves chemical modification of a protein after its translation. It is one of the later steps in protein biosynthesis and thus gene expression. During protein synthesis, 20 different amino acids can be incorporated to become a protein. After translation, the posttranslational modification of amino acids extends the range of functions of the protein by attaching it to other biochemical functional groups such as acetate, phosphate, various lipids and carbohydrates, by changing the chemical nature of an amino acid (e.g. citrullination) or by making structural changes, like the formation of disulfide bridges. Also, enzymes may remove amino acids from the amino end of the protein, or cut the peptide chain in the middle. For instance, the peptide hormone insulin is cut twice after disulfide bonds are formed, and a propeptide is removed from the middle of the chain; the resulting protein consists of two polypeptide chains connected by disulfide bond.

Figure 2 showing the post translation modification in insulin protein (wikipedia) Differences between translation in Eukaryotes and Prokaryotes RNA is usually translated while it is being transcribed since both transcription and translation takes place in the cytoplasm. Transcription of the eukaryotic mRNA occurs in the nucleus, mRNA then moves to the cytoplasm for translation. Another difference is that eukaryotic mRNA must be modified by capping and intron splicing before it can be used to make protein. However, in prokaryotes, the mRNA usually doesnt need much modification and that is why it is able to undergo translation before transcription is done. Most prokaryotic mRNA molecules often contain transcripts of several genes because of clustering of genes related by functions (operons) thus more than one protein is usually expressed by these mRNas. The Eukaryotic mRNA usually specifies only a single protein.