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  2. EF-Tu - Wikipedia

    en.wikipedia.org/wiki/EF-Tu

    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.

  3. Eukaryotic translation - Wikipedia

    en.wikipedia.org/wiki/Eukaryotic_translation

    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 ...

  4. Aminoacyl-tRNA - Wikipedia

    en.wikipedia.org/wiki/Aminoacyl-tRNA

    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.

  5. Elongation factor - Wikipedia

    en.wikipedia.org/wiki/Elongation_factor

    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).

  6. EF-G - Wikipedia

    en.wikipedia.org/wiki/EF-G

    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 .

  7. Bacterial translation - Wikipedia

    en.wikipedia.org/wiki/Bacterial_translation

    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 ...