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Related Experiment Videos

Negatively charged residues in the IgM stop-transfer effector sequence regulate transmembrane polypeptide

D Falcone1, H Do, A E Johnson

  • 1Department of Biochemistry, McMaster University, Hamilton, Ontario L8N 3Z5, Canada.

The Journal of Biological Chemistry
|November 24, 1999
PubMed
Summary

Stop-transfer effectors (STE) guide transmembrane protein biogenesis. Negative charges within STEs, not specific amino acids, dictate transmembrane topology, revealing a novel mechanism for protein insertion into the endoplasmic reticulum membrane.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Protein Trafficking

Background:

  • Transmembrane proteins are essential cellular components requiring precise insertion into membranes.
  • Stop-transfer effectors (STEs) are non-hydrophobic sequences involved in halting protein translocation across the endoplasmic reticulum membrane.

Purpose of the Study:

  • To investigate the mechanism by which STE sequences mediate stop-transfer during transmembrane protein biogenesis.
  • To identify the key features within STE sequences responsible for recognizing and interacting with the translocation machinery.

Main Methods:

  • Construction of fusion proteins incorporating variants of a murine IgM STE with a hydrophobic sequence.
  • Analysis of transmembrane protein topology (Type I and Type II) using reporter constructs.

Related Experiment Videos

  • Photocross-linking assays to identify proteins interacting with functional STE sequences.

    • Main Results:

    • Transmembrane topology was found to be insensitive to most amino acid substitutions within the STE but directly correlated with the number of negative charges.
    • STE sequences demonstrated functional flexibility, mediating both Type I and Type II transmembrane topologies depending on their location relative to the reporter.
    • Photocross-linking identified two novel membrane proteins associated with the translocon that interact with STE sequences.

    Conclusions:

    • STE function relies on recognizing a broad structural feature, primarily driven by negatively charged residues, to halt translocation and initiate membrane integration.
    • The STE sequence's ability to function on either side of the endoplasmic reticulum membrane highlights its adaptability in protein insertion.
    • The newly identified translocon-associated proteins are likely crucial for STE recognition and facilitating their role in transmembrane protein biogenesis.