DNA Translation:DNA To Protein
DNA Translation:DNA To Protein
Translation refers to the process of polymerisation of amino acids to form a polypeptide.The order of the amino acids is defined by the sequence of bases in the m-RNA.Formation of a peptide bond requires energy, therefore in the first step amino acids are activated in the presence of ATP.
Step1: Activation of amino acids
Amino acids react with ATP to form amino acid –AMP complex and pyrophosphate.
The reaction is catalysed by a specific amino acid -activating enzyme called aminoacyl-tRNA synthetase.
Step 2: Charging of tRNA
The amino acid -AMP -enzyme complex joins the amino acid binding site to its specific tRNA where the COOH group of the amino acid binds to the -OH group of the tRNA.
tRNA +amino acid get separated from enzyme+AMP.
tRNA +amino acid complexis called charged tRNA.
Step3:Activation of Ribosome
The small and the large subunits of ribosomes must be joined together for protein synthesis , this is brought by mRNA chain.
The mRNA chain joins the small ribosomal subunit by first codon through base pairing with appropriate sequence on rRNA.This is called the initiation complex.
The large subunit later joins the small subunit forming the active ribosome.
Step 4: Polypeptide Formation
Initiation of polypeptide chain
Inititation stage brings together an mRNA , a tRNA bearing the first amino acid of the polypeptide ,and the two subunits of the ribosome.Union of all these components forms translation initiation complex.
On the mRNA lies the initiator codon ,AUG, which signals the start of translation.
The initiator tRNA joins the initiator codon by its anticodon through hydrogen bonds.
It carries methionine in eukaryotes.At this stage initiator tRNA lies at the P site of the ribosome, and at the A site is left vacant to let another charged tRNA to enter.
Elongation of the polypeptide chain
In the elongationstage of translation,amino acids are added one by one to the first amino acid(methionine, present at P site).
A charged tRNA enters the ribosome at the A site(say proline). GTP is hydrolyzed in this step.
The amino acid(methionine) on tRNA at the P site and the newly arrived amino acid on tRNA at the A site join by a peptide bond.The reaction is catalyzed by peptidal transferase.
In the peptide bond formation ,the linkage between the first amino acid (methionine)and its tRNA is broken,and the -COOH group(of methionine) now forms a peptide bond with the NH2 group of the second amino acid.(proline).Which means that the second tRNA carries a dipeptide (proline and methionine) and first tRNA is without amino acid(carried methionine earlier).
Translocation
The tRNA at the A site (carring a dipeptide)moves to the P site .This process is translocation.It requires energy.
As the tRNA translocates to the P site ,its anti codon keeps bonded to the mRNA codon,so that mRNA moves along with it and brings its next codon to the A site. In the meantime .the uncharged tRNA shifts from the P site to mixed pool of tRNAs in the cytoplasm.
The next cycle starts, till the whole mRNA is translated.
Step 5: The termination of the polypeptide Chain
At the end of the mRNA chain there is a stop codon(UAA,UAG,UGA)
The stop codon reaches the A site but is not read.
A protein called the release factor joins the stop codon in theA site .It adds water molecule to thepolypeptide chain.This hydrolyses (cleaves)the completed polypeptide from the t RNA that is at the P site.
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