Rac

Initiation codon

4 15.20 Shine-Dalgarno consensus sequences in mRNA are required for the attachment of the small subunit of the ribosome. The Shine-Dalgarno sequences are complementary to a sequence of nucleotides found near the 3' end of 16S rRNA in the small subunit of the ribosome. These complementary nucleotides base pair during the initiation of translation.

subunit of the ribosome to join the initiation complex. The molecule of GTP (provided by IF-2) is hydrolyzed to guanosine diphosphate (GDP), and IF-1 and IF-2 depart (see Figure 15.19d). When the large subunit has joined the initiation complex, it is called the 70S initiation complex.

Similar events take place in the initiation of translation in eukaryotic cells, but there are some important differences. In bacterial cells, sequences in 16S rRNA of the small subunit of the ribosome bind to the Shine-Dalgarno sequence in mRNA; this binding positions the ribosome over the start codon. No analogous consensus sequence exists in eukaryotic mRNA. Instead, the cap at the 5' end of eukaryotic mRNA plays a critical role in the initiation of translation. The small subunit of the eukaryotic ribosome, with the help of initiation factors, recognizes the cap and binds there; the small subunit then migrates along (scans) the mRNA until it locates the first AUG codon. The identification of the start codon is facilitated by the presence of a consensus sequence (called the Kozak sequence) that surrounds the start codon:

Start codon

Another important difference is that eukaryotic initiation requires more initiation factors. Some factors keep the ribosomal subunits separated, just as IF-3 does in bacterial cells. Others recognize the 5' cap on mRNA and allow the small subunit of the ribosome to bind there. Still others possess RNA helicase activity, which is used to unwind secondary structures that may exist in the 5' untranslated region of mRNA, allowing the small subunit to move down the mRNA until the initiation codon is reached. Other initiation factors help bring the initiator tRNA and methionine (Met-tRNAfMet) to the initiation complex.

The poly(A) tail at the 3' end of eukaryotic mRNA also plays a role in the initiation of translation. Proteins that attach to the poly(A) tail interact with proteins that bind to the 5' cap, enhancing the binding of the small subunit of the ribosome to the 5' end of the mRNA. This interaction between the 5' cap and the 3' tail suggests that the mRNA bends backward during the initiation of translation, forming a circular structure ( < Figure 15.21). A few eukaryotic mRNAs contain internal ribosome entry sites, where ribosomes can bind directly without first attaching to the 5' cap.

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