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Translation is one of the key energy consumers in cells, hence it is strictly regulated. Numerous mechanisms have evolved that control and regulate translation in eukaryotes as well as prokaryotes. Regulation of translation can impact the global rate of protein synthesis which is closely coupled to the metabolic and proliferative state of a cell.
A basic model of protein synthesis that takes into account all eight 'elementary' processes has been developed, [23] following the paradigm that "useful models are simple and extendable". [27] The simplest model M0 is represented by the reaction kinetic mechanism (Figure M0).
The eIF2 alpha subunit is characterized by an OB-fold domain and two beta strands. This subunit helps to regulate translation, as it becomes phosphorylated to inhibit protein synthesis. [2] The eIF4F complex supports the cap-dependent translation initiation process and is composed of the initiation factors eIF4A, eIF4E, and eIF4G.
Protein synthesis is a very similar process for both prokaryotes and eukaryotes but there are some distinct differences. [1] Protein synthesis can be divided broadly into two phases: transcription and translation. During transcription, a section of DNA encoding a protein, known as a gene, is converted into a molecule called messenger RNA (mRNA).
Based on the Watson-Crick model, he envisaged that the DNA itself is a direct template for protein synthesis. [18] Assuming that the four bases of DNA could produce 20 different combinations as triplets, he suggested that the different amino acids must correspond to a twenty-letter alphabet of the nucleotide sequence. [ 19 ]
Initiation of translation in bacteria involves the assembly of the components of the translation system, which are: the two ribosomal subunits (50S and 30S subunits); the mature mRNA to be translated; the tRNA charged with N-formylmethionine (the first amino acid in the nascent peptide); guanosine triphosphate (GTP) as a source of energy, and the three prokaryotic initiation factors IF1, IF2 ...
Phosphorylation is highly effective for controlling the enzyme activity and is the most common change after translation. [ 2 ] Many eukaryotic and prokaryotic proteins also have carbohydrate molecules attached to them in a process called glycosylation , which can promote protein folding and improve stability as well as serving regulatory functions.
The ribosomal P-site plays a vital role in all phases of translation. Initiation involves recognition of the start codon (AUG) by initiator tRNA in the P-site, elongation involves passage of many elongator tRNAs through the P site, termination involves hydrolysis of the mature polypeptide from tRNA bound to the P-site, and ribosome recycling involves release of deacylated tRNA.