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EF-Tu (elongation factor thermo unstable) is a prokaryotic elongation factor responsible for catalyzing the binding of an aminoacyl-tRNA (aa-tRNA) to the ribosome. It is a G-protein , and facilitates the selection and binding of an aa-tRNA to the A-site of the ribosome.
The elongation and membrane targeting stages of eukaryotic translation. The ribosome is green and yellow, the tRNAs are dark-blue, and the other proteins involved are light-blue. Elongation depends on eukaryotic elongation factors. At the end of the initiation step, the mRNA is positioned so that the next codon can be translated during the ...
The elongation factor EF-Tu has been shown to stabilize the bond by preventing weak acyl linkages from being hydrolyzed. [ 12 ] All together, the actual stability of the ester bond influences the susceptibility of the aa-tRNA to hydrolysis within the body at physiological pH and ion concentrations.
In normal mRNA translation, the ribosome binds to the transcript and begins amino acid chain elongation. It continues on until it reaches the location of the exon junction complex, which it then displaces. Next, translation is complete when the ribosome reaches a termination codon.
Elongation is the most rapid step in translation. [3] In bacteria , it proceeds at a rate of 15 to 20 amino acids added per second (about 45-60 nucleotides per second). [ citation needed ] In eukaryotes the rate is about two amino acids per second (about 6 nucleotides read per second).
EF-G (elongation factor G, historically known as translocase) is a prokaryotic elongation factor involved in mRNA translation. As a GTPase , EF-G catalyzes the movement (translocation) of transfer RNA (tRNA) and messenger RNA (mRNA) through the ribosome .
The corresponding mechanisms are primarily targeted on the control of ribosome recruitment on the initiation codon, but can also involve modulation of peptide elongation, termination of protein synthesis, or ribosome biogenesis. While these general concepts are widely conserved, some of the finer details in this sort of regulation have been ...
The eEF1A1 protein is an isoform of the eEF-1 complex alpha subunit, an elongation factor protein, a GTPase, and an actin bundling protein. [7] [8] [9] [14] As an elongation factor, it is known to mediate the recruitment of aminoacyl-tRNA to the A-site of the 80S ribosome during protein synthesis.
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