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Questions and Answers

What is the role of chaperones in protein folding?

  • They provide a structural framework for proteins.
  • They assist in the proper folding of misfolded proteins using ATP. (correct)
  • They degrade improperly folded proteins immediately.
  • They chemically modify proteins to enhance their function.
  • Which statement about hydrophobic amino acids in proteins is true?

  • They facilitate interactions with small molecules.
  • They are essential for the phosphorylation of proteins.
  • They are always located on the protein surface.
  • They contribute to protein stability by being buried in the core. (correct)
  • What is the consequence of improperly folded proteins?

  • They enhance cellular activities.
  • They increase the protein synthesis rate.
  • They can aggregate and become toxic to cells. (correct)
  • They are always recognized and corrected by ribosomes.
  • What is the function of the proteasome?

    <p>To degrade misfolded proteins marked by hydrophobic residues. (B)</p> Signup and view all the answers

    How do heat-shock proteins (Hsp) respond to cellular stress?

    <p>They are synthesized in larger quantities. (B)</p> Signup and view all the answers

    What effect does the presence of exposed hydrophobic residues have on a protein?

    <p>It marks the protein for degradation by the proteasome. (A)</p> Signup and view all the answers

    Which of the following statements is false regarding post-translational regulation?

    <p>All proteins must undergo chemical modification after synthesis. (A)</p> Signup and view all the answers

    Which factor is least likely to interfere with protein folding?

    <p>Presence of molecular chaperones. (D)</p> Signup and view all the answers

    Which of the following processes is NOT involved in the regulation of the proteome?

    <p>Chromatin Remodeling (C)</p> Signup and view all the answers

    What role does protein phosphorylation play in cellular regulation?

    <p>It activates or deactivates proteins. (A)</p> Signup and view all the answers

    What initiates the process of translation in eukaryotes?

    <p>Formation of the ribosomal complex with eIF2. (A)</p> Signup and view all the answers

    Which mechanism is NOT a form of translational regulation in prokaryotes?

    <p>Polyadenylation of mRNA (D)</p> Signup and view all the answers

    The role of aconitase in eukaryotic translation is to:

    <p>Block translation when iron levels are low. (C)</p> Signup and view all the answers

    Which of the following components plays a crucial role in the formation of the eukaryotic initiation complex?

    <p>eIF2 complexed with GTP (A)</p> Signup and view all the answers

    How does the phosphorylation of eIF2 impact translation?

    <p>It sequesters eIF2B, leading to reduced translation. (C)</p> Signup and view all the answers

    Which of these mechanisms is indicative of post-translational regulation?

    <p>Phosphorylation of proteins. (A)</p> Signup and view all the answers

    What is the main function of molecular chaperons in protein synthesis?

    <p>To assist in protein folding and modification. (A)</p> Signup and view all the answers

    Which sequence is specifically mentioned as being important in prokaryotic translational regulation?

    <p>Shine-Dalgarno sequence (A)</p> Signup and view all the answers

    What is the potential consequence of the environmental stress on protein expression?

    <p>It may induce the upregulation of specific stress response proteins. (D)</p> Signup and view all the answers

    In eukaryotic cells, which process does NOT contribute to gene expression regulation?

    <p>Elongation of the mRNA (D)</p> Signup and view all the answers

    What distinguishes regulatory GTP-binding proteins from other proteins?

    <p>They are switched on and off by phosphate groups. (C)</p> Signup and view all the answers

    Study Notes

    Genome Expression Regulation

    • The proteome reflects the expression of the genome and transcriptome
    • Proteome differences between tissues are represented with red (common proteins) and blue (tissue specific proteins)
    • The regulation of genome expression involves multiple steps: organization, transcription, RNA splicing, translation, protein sorting, and post-translational modification

    Translational Regulation

    • Prokaryotes and eukaryotes use translational control mechanisms
    • Prokaryotes use a Shine-Dalgarno (SD) sequence upstream of the AUG start codon for translation initiation
    • Translational regulation in prokaryotes can involve:
      • RNA binding proteins blocking access to the SD sequence
      • Temperature-regulated RNA structures (e.g., Listeria monocytogenes)
      • Riboswitches (e.g., S-adenosyl methionine)
      • Antisense RNA (e.g., iron storage proteins) which base-pairs with mRNA to block the SD sequence

    Translational Regulation: Eukaryotes

    • Eukaryotes lack Shine-Dalgarno sequences
    • Repressor proteins can bind near the initiator AUG to inhibit translation, or interfere with 5' cap and 3' poly-A tail interactions
    • Small RNA molecules (microRNAs or miRNAs) regulate eukaryotic translation
    • Eukaryotic initiation factors (eIFs) regulate translation:
      • eIF2 plays a crucial role in translation initiation, forming a complex with GTP and initiator tRNA
      • GTP hydrolysis causes a conformational change in eIF2, leading to its release as an inactive GDP-bound form
      • Reactivation of eIF2 requires eIF2B, a guanine nucleotide exchange factor (GEF) that promotes GDP-GTP exchange
      • However, phosphorylation of eIF2 can sequester eIF2B, forming an inactive complex and inhibiting translation

    Post-Translational Regulation: Proteins

    • Proteins undergo post-translational modifications to become functional, including:
      • Proper folding into 3-D structure
      • Covalent modifications with chemical groups (e.g., sugars, phosphate)
      • Interactions with other proteins and small molecules (cofactors)

    Post-Translational Regulation: Protein Folding

    • Hydrophobic amino acids are buried in the protein interior core
    • Folding can begin during translation for some proteins or after synthesis
    • Chaperones (e.g., Hsp70 and Hsp60) assist with protein folding:
      • Interact with exposed hydrophobic residues of misfolded proteins
      • Utilize ATP hydrolysis for proper folding
    • Misfolded proteins can aggregate and become toxic
    • The proteasome is a protein degrading apparatus that targets misfolded proteins:
      • Misfolded proteins display exposed hydrophobic residues, leading to proteasome recognition
      • Proteasome degradation competes with chaperone interactions, and the longer a protein takes to fold, the higher the chance of degradation

    Review Question

    • Treatment with HSP inhibitors should reduce protein degradation
    • Treatment with an iron chelator should decrease ferritin transcription
    • Treatment with a miRNA complementary to eIF2B should result in an increase in transcription

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