Question:
During the formation of amino acyl tRNA, the amino acid is attached covalently to which part of tRNA?
During the formation of amino acyl tRNA, the amino acid is attached covalently to which part of tRNA?
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Remember the structural features of tRNA:
- Acceptor Arm: Ends in 3'-CCA, where the terminal Adenosine binds the amino acid.
- Anticodon Loop: Recognizes the mRNA codon.
- T\(\mathbf{\psi}\)C Loop: Contains Pseudouridine (\(\psi\)).
- D Loop: Contains Dihydrouridine (D).
- Acceptor Arm: Ends in 3'-CCA, where the terminal Adenosine binds the amino acid.
- Anticodon Loop: Recognizes the mRNA codon.
- T\(\mathbf{\psi}\)C Loop: Contains Pseudouridine (\(\psi\)).
- D Loop: Contains Dihydrouridine (D).
Updated On: Jul 21, 2026
- Cytosine residue of -CCA sequence of acceptor arm of tRNA.
- Adenosine residue of -CCA sequence of acceptor arm of tRNA.
- Pseudouridine residue of acceptor arm of tRNA.
- Dihydrouridine residue of acceptor arm of tRNA.
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The Correct Option is B
Solution and Explanation
Step 1: Understanding the Concept:
Translation requires the activation of amino acids by coupling them to their corresponding tRNA molecules.
This "charging" process is catalyzed by specific aminoacyl-tRNA synthetase enzymes, forming an aminoacyl-tRNA.
Step 2: Detailed Explanation:
All transfer RNA (tRNA) molecules share a conserved tertiary L-shaped structure.
At their 3' end, they contain a highly conserved, single-stranded nucleotide sequence: 5'-CCA-3'.
This region is known as the acceptor stem or acceptor arm.
During the aminoacylation reaction, the enzyme aminoacyl-tRNA synthetase first activates the amino acid by reacting it with ATP to form aminoacyl-AMP.
The enzyme then transfers the aminoacyl group to the terminal Adenosine (A) residue of the 3'-CCA sequence.
Specifically, the carboxyl group of the amino acid forms a high-energy ester bond with either the 2'-hydroxyl (\(-\text{OH}\)) or 3'-hydroxyl (\(-\text{OH}\)) group of the ribose sugar of this terminal adenosine residue.
This covalent linkage activates the amino acid for subsequent peptide bond formation during translation.
The cytosine residues of the -CCA sequence (A), pseudouridine loop (C), and dihydrouridine loop (D) are not the sites of covalent attachment for the amino acid.
Step 3: Final Answer:
The amino acid is attached covalently to the Adenosine residue of the -CCA sequence of the acceptor arm of tRNA.
Translation requires the activation of amino acids by coupling them to their corresponding tRNA molecules.
This "charging" process is catalyzed by specific aminoacyl-tRNA synthetase enzymes, forming an aminoacyl-tRNA.
Step 2: Detailed Explanation:
All transfer RNA (tRNA) molecules share a conserved tertiary L-shaped structure.
At their 3' end, they contain a highly conserved, single-stranded nucleotide sequence: 5'-CCA-3'.
This region is known as the acceptor stem or acceptor arm.
During the aminoacylation reaction, the enzyme aminoacyl-tRNA synthetase first activates the amino acid by reacting it with ATP to form aminoacyl-AMP.
The enzyme then transfers the aminoacyl group to the terminal Adenosine (A) residue of the 3'-CCA sequence.
Specifically, the carboxyl group of the amino acid forms a high-energy ester bond with either the 2'-hydroxyl (\(-\text{OH}\)) or 3'-hydroxyl (\(-\text{OH}\)) group of the ribose sugar of this terminal adenosine residue.
This covalent linkage activates the amino acid for subsequent peptide bond formation during translation.
The cytosine residues of the -CCA sequence (A), pseudouridine loop (C), and dihydrouridine loop (D) are not the sites of covalent attachment for the amino acid.
Step 3: Final Answer:
The amino acid is attached covalently to the Adenosine residue of the -CCA sequence of the acceptor arm of tRNA.
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