Aminoacyl-tRNA Synthetases in Translation
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Questions and Answers

What is the primary reason for the high conservation of aminoacyl-tRNA synthetases across species?

  • To facilitate the evolution of new protein functions
  • To optimize the energy efficiency of protein synthesis
  • To ensure the correct amino acid attachment to tRNA (correct)
  • To maintain the diversity of protein sequences
  • What is the main purpose of the pre-transfer editing mechanism in aminoacyl-tRNA synthetases?

  • To hydrolyze incorrectly charged tRNA molecules (correct)
  • To increase the specificity of tRNA recognition
  • To proofread the amino acid sequence of proteins
  • To enhance the rate of amino acid activation
  • What is the intermediate formed during the amino acid activation reaction catalyzed by aminoacyl-tRNA synthetases?

  • tRNA-adenylate
  • Aminoacyl-adenylate (correct)
  • Amino acid-adenylate complex
  • Aminoacyl-tRNA
  • What is the primary region of the tRNA molecule recognized by aminoacyl-tRNA synthetases?

    <p>Acceptor stem</p> Signup and view all the answers

    What is the consequence of defective editing mechanisms in aminoacyl-tRNA synthetases?

    <p>Increased error frequency in protein sequences</p> Signup and view all the answers

    What is the primary function of the peripheral domains of aminoacyl-tRNA synthetases?

    <p>To provide additional functional diversity</p> Signup and view all the answers

    What is the energy source that drives the amino acid activation reaction?

    <p>Energy from the destruction of PPi</p> Signup and view all the answers

    What is the function of the enzyme Met-tRNA transformilase?

    <p>To introduce the formyl group into the tRNA</p> Signup and view all the answers

    What is the difference between Class I and Class II aminoacyl-tRNA synthetases?

    <p>Class I synthetases transfer the amino acid to the 2'OH of the tRNA, while Class II synthetases transfer to the 3'OH</p> Signup and view all the answers

    What is the amino acid that is modified to become selenocysteine?

    <p>Serine</p> Signup and view all the answers

    What is the region of the tRNA molecule recognized by aminoacyl-tRNA synthetases?

    <p>The acceptor stem</p> Signup and view all the answers

    What is the consequence of the amino acid activation reaction?

    <p>The formation of an aminoacyl-AMP complex</p> Signup and view all the answers

    What is the characteristic of the amino acid selenocysteine?

    <p>It is synthesized from serine</p> Signup and view all the answers

    What is the structure of Class I aminoacyl-tRNA synthetases?

    <p>Monomeric</p> Signup and view all the answers

    What is the purpose of the union of the amino acid to the tRNA?

    <p>To facilitate the formation of the peptide bond</p> Signup and view all the answers

    What is the result of the breakdown of the pyrophosphate in the amino acid activation reaction?

    <p>Formation of 2 monophosphates</p> Signup and view all the answers

    What is the location of the aminoacyl-tRNA synthetases in eukaryotes?

    <p>Both in the cytoplasm and mitochondria</p> Signup and view all the answers

    What is the role of the aminoacyl-tRNA synthetases in protein synthesis?

    <p>To form a covalent bond between the amino acid and the tRNA</p> Signup and view all the answers

    What is the purpose of the ATP in the amino acid activation reaction?

    <p>To activate the amino acid by forming a 5'-aminoacyl adenylate</p> Signup and view all the answers

    How many different aminoacyl-tRNA synthetases can form a complex in the cytoplasm?

    <p>Up to 11</p> Signup and view all the answers

    What codifies the mitochondrial aminoacyl-tRNA synthetases?

    <p>Nuclear genes</p> Signup and view all the answers

    What is the outcome of the attack of the carboxyl group of the amino acid on the ATP?

    <p>Formation of a 5'-aminoacyl adenylate</p> Signup and view all the answers

    In some bacteria and archaea, which amino acid is charged onto tRNA?

    <p>Glutamate</p> Signup and view all the answers

    What is the role of the protein that recognizes the tRNA of selenocysteine and attracts it to the ribosome?

    <p>Factor of elongation</p> Signup and view all the answers

    What is the codon recognized by the termination factor?

    <p>UGA</p> Signup and view all the answers

    Which amino acid is not ancestral, but is coded by a codon that was previously used by another amino acid?

    <p>Glutamine</p> Signup and view all the answers

    In eukaryotes, what is the state of glutamine?

    <p>Free</p> Signup and view all the answers

    What is the role of the aminotransferase in glutamine synthesis?

    <p>Transforms glutamate into glutamine</p> Signup and view all the answers

    Which protein participates in antioxidant reactions and contains selenocysteine?

    <p>Glutathione peroxidase</p> Signup and view all the answers

    What is the intermediate in the reaction catalyzed by selenocysteine synthase?

    <p>Seril-tRNASec</p> Signup and view all the answers

    Which amino acid has its own enzyme that charges it onto its specific tRNA?

    <p>Pirrolisine</p> Signup and view all the answers

    Study Notes

    Aminoacyl-tRNA Synthetases

    Evolutionary Conservation

    • Aminoacyl-tRNA synthetases are highly conserved across species, indicating their essential role in translation.
    • The core catalytic domain is highly conserved, while the peripheral domains show more variation.
    • Conservation of amino acid sequences and structures across species highlights their importance in maintaining protein synthesis fidelity.

    Editing Mechanisms

    • Aminoacyl-tRNA synthetases have built-in editing mechanisms to ensure correct amino acid attachment to tRNA.
    • Editing mechanisms include:
      1. Pre-transfer editing: hydrolysis of incorrectly charged tRNA molecules.
      2. Post-transfer editing: proofreading and correction of mischarged tRNA molecules.
    • Editing mechanisms help maintain the fidelity of protein synthesis by reducing errors.

    Amino Acid Activation

    • Aminoacyl-tRNA synthetases catalyze the reaction between amino acids and tRNA molecules.
    • The reaction involves the formation of an aminoacyl-adenylate intermediate, which is then transferred to the tRNA molecule.
    • Amino acid activation is a two-step process:
      1. Amino acid is adenylated, forming an aminoacyl-adenylate intermediate.
      2. The intermediate is then transferred to the tRNA molecule, forming an aminoacyl-tRNA molecule.

    tRNA Recognition

    • Aminoacyl-tRNA synthetases recognize specific tRNA molecules through interactions with the tRNA acceptor stem and anticodon.
    • Recognition is based on the sequence and structure of the tRNA molecule, ensuring correct pairing with the corresponding amino acid.
    • tRNA recognition is crucial for maintaining the fidelity of protein synthesis.

    Error Correction

    • Aminoacyl-tRNA synthetases have error correction mechanisms to prevent incorrect amino acid incorporation.
    • Errors can occur due to:
      • Misactivated amino acids.
      • Incorrect tRNA recognition.
    • Error correction mechanisms include:
      • Hydrolysis of incorrectly charged tRNA molecules.
      • Proofreading and correction of mischarged tRNA molecules.
    • Error correction mechanisms help maintain the fidelity of protein synthesis.

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    Description

    Learn about the crucial role of aminoacyl-tRNA synthetases in protein synthesis, including their evolutionary conservation, editing mechanisms, amino acid activation, tRNA recognition, and error correction mechanisms. Understand how these enzymes ensure the fidelity of protein synthesis.

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