Search results
Results From The WOW.Com Content Network
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 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.
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.
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 rate of semiconservative DNA replication in a living cell was first measured as the rate of the T4 phage DNA strand elongation in phage-infected E. coli. [10] During the period of exponential DNA increase at 37 °C, the rate of strand elongation was 749 nucleotides per second.
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.
Simple diagram of transcription elongation. One strand of the DNA, the template strand (or noncoding strand), is used as a template for RNA synthesis. As transcription proceeds, RNA polymerase traverses the template strand and uses base pairing complementarity with the DNA template to create an RNA copy (which elongates during the traversal).
As RF1/2 sits in the A site of the ribosome, domains 2, 3, and 4 occupy the space that tRNAs load into during elongation. Stop codon recognition activates the RF, promoting a compact to open conformation change, [ 15 ] sending the GGQ motif to the peptidyl transferase center (PTC) next to the 3′ end of the P-site tRNA.