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Eukaryotic translation is the biological process by which messenger RNA is translated into proteins in eukaryotes. It consists of four phases: initiation, elongation, termination, and recapping. It consists of four phases: initiation, elongation, termination, and recapping.
The process of amino acid building to create protein in translation is a subject of various physic models for a long time starting from the first detailed kinetic models such as [26] or others taking into account stochastic aspects of translation and using computer simulations. Many chemical kinetics-based models of protein synthesis have been ...
Most common elongation factors in prokaryotes are EF-Tu, EF-Ts, EF-G. [1] Bacteria and eukaryotes use elongation factors that are largely homologous to each other, but with distinct structures and different research nomenclatures. [2] Elongation is the most rapid step in translation. [3]
Due to the fact that translation elongation is an irreversible process, there are few known mechanisms of its regulation. However, it has been shown that translational efficiency is reduced via diminished tRNA pools, which are required for the elongation of polypeptides.
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.
Once translation initiation is complete, the first aminoacyl tRNA is located in the P/P site, ready for the elongation cycle described below. During translation elongation, tRNA first binds to the ribosome as part of a complex with elongation factor Tu or its eukaryotic or archaeal counterpart. This initial tRNA binding site is called the A/T site.
The elongation phase of translation is promoted by three universal elongation factors, EF-Tu, EF-Ts, and EF-G. [9] EF-P was discovered in 1975 by Glick and Ganoza, [10] as a factor that increased the yield of peptide bond formation between initiator fMet-tRNA(fMet) and a mimic of aa-tRNA, puromycin (Pmn). The low yield of product formation in ...
Alterations in translation of mRNA into proteins rapidly modulates the proteome without changing upstream steps such as transcription, pre-mRNA splicing, and nuclear export. [1] The strict regulation of translation in both space and time is in part governed by cis-regulatory elements located in 5′ mRNA transcript leaders (TLs) and 3 ...