Step 1: Charging of tRNA, how it happens:
The amino acid is first activated. The enzyme aminoacyl-tRNA synthetase joins the amino acid to ATP and forms an amino acid-AMP complex.
The activated amino acid is then moved to the \( 3^{\prime} \) (CCA) end of its own tRNA. The product is aminoacyl-tRNA, also called a charged tRNA.
Step 2: Charging of tRNA, why it is essential:
A tRNA cannot carry an amino acid on its own. Without charging, the amino acid would never reach the ribosome.
The anticodon of the charged tRNA pairs with the mRNA codon, so each codon brings in the correct amino acid. The energy stored in the bond also pays for the peptide bond.
Step 3: Ribosome as a catalyst in bacteria:
The 23S rRNA of the large subunit works as a ribozyme. It catalyses the formation of the peptide bond between the amino acids held at the two sites of the large subunit.
Step 4: Binding of the ribosomal units to mRNA:
In the inactive state the ribosome stays as two separate subunits. The small subunit first meets the mRNA and binds near the start codon AUG.
The initiator tRNA (carrying methionine) pairs with AUG. Then the large subunit joins the small subunit and forms the complete ribosome. Translation moves on to elongation.
Step 5: Untranslated regions (UTRs):
UTRs lie on both ends of the mRNA. One is at the \( 5^{\prime} \) end, before the start codon. The other is at the \( 3^{\prime} \) end, after the stop codon.
They are not translated into protein. They are needed for efficient translation.
Final Answer:
All four parts are answered: tRNA charging by aminoacyl-tRNA synthetase, 23S rRNA as the catalyst, small subunit first and then large subunit on AUG, and UTRs at the \( 5^{\prime} \) and \( 3^{\prime} \) ends.