The following are steps that occur when a protein is targeted for synthesis on the endoplasmic reticulum (ER). Which of the following indicates the correct sequence for the signal mechanism that targets proteins for the ER? The SRP leaves and polypeptide synthesis resumes, with simultaneous translocation across the membrane. Polypeptide synthesis begins on a free ribosome in the cytosol. An SRP binds to the signal peptide, halting synthesis momentarily. The rest of the completed polypeptide leaves the ribosome and folds into its final conformation. The SRP binds to a receptor protein in the ER membrane that is part of a protein complex that forms a pore. The signal peptide is cleaved by an enzyme in the receptor protein complex. A. 2, 3, 5, 1, 6, 4 B. 2 ,3, 5, 6, 1, 4 C. 3, 1, 6, 5, 2, 4 D. 3, 2, 1, 5, 6, 4

Human Physiology: From Cells to Systems (MindTap Course List)
9th Edition
ISBN:9781285866932
Author:Lauralee Sherwood
Publisher:Lauralee Sherwood
Chapter2: Cell Physiology
Section: Chapter Questions
Problem 11RE
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The following are steps that occur when a protein is targeted for synthesis on the endoplasmic reticulum (ER). Which of the following indicates the correct sequence for the signal mechanism that targets proteins for the ER?

  1. The SRP leaves and polypeptide synthesis resumes, with simultaneous translocation across the membrane.
  2. Polypeptide synthesis begins on a free ribosome in the cytosol.
  3. An SRP binds to the signal peptide, halting synthesis momentarily.
  4. The rest of the completed polypeptide leaves the ribosome and folds into its final conformation.
  5. The SRP binds to a receptor protein in the ER membrane that is part of a protein complex that forms a pore.
  6. The signal peptide is cleaved by an enzyme in the receptor protein complex.
    A. 2, 3, 5, 1, 6, 4
    B. 2 ,3, 5, 6, 1, 4
    C. 3, 1, 6, 5, 2, 4
    D. 3, 2, 1, 5, 6, 4
Expert Solution
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Answer:

Introduction: Proteins are nourished into the ER at the time of translation if they consist of an amino sequence known as a signal peptide.

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