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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 ...
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).
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 .
Elongation factors exist in all three domains of life with similar function on the ribosome. The eukaryotic and archeal homologs of EF-G are eEF2 and aEF2, respectively. In bacteria (and some archaea), the fusA gene that encodes EF-G is found within the conserved str gene with the sequence 5′ - rpsL - rpsG - fusA - tufA - 3′. [ 2 ]
Elongation of the polypeptide chain involves addition of amino acids to the carboxyl end of the growing chain. The growing protein exits the ribosome through the polypeptide exit tunnel in the large subunit. [10] Elongation starts when the fMet-tRNA enters the P site, causing a conformational change which opens the A site for the new aminoacyl ...
The elongation phase starts once assembly of the elongation complex has been completed, and progresses until a termination sequence is encountered. [1] The post-initiation movement of RNA polymerase is the target of another class of important regulatory mechanisms.
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.