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Signal sequence processing in rough microsomes

F Lyko1, B Martoglio, B Jungnickel

  • 1ZMBH, Universität Heidelberg, Germany.

The Journal of Biological Chemistry
|August 25, 1995
PubMed
Summary
This summary is machine-generated.

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The fate of cleaved signal peptides from secretory proteins was investigated. Researchers found that signal peptides are further processed and eventually released into the cytosol.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Protein Biochemistry

Background:

  • Secretory proteins utilize signal sequences for endoplasmic reticulum translocation.
  • Signal sequences are typically cleaved during translocation into the ER lumen.
  • The subsequent fate and processing of these cleaved signal sequences remain largely uncharacterized.

Purpose of the Study:

  • To elucidate the post-cleavage fate of signal sequences.
  • To investigate the processing and localization of cleaved signal peptides.
  • To identify the molecular machinery involved in signal peptide processing.

Main Methods:

  • Utilized a synchronized in vitro translocation system.
  • Employed preprolactin as a model secretory protein.

Related Experiment Videos

  • Reconstituted translocation vesicles with key protein components (Sec61, SRP receptor, signal peptidase complex).

    • Main Results:

    • The cleaved signal peptide of preprolactin undergoes further processing near its COOH terminus.
    • The processed signal peptide fragment initially accumulates in the microsomal fraction.
    • This fragment is subsequently released into the cytosol over time.
    • Signal peptide cleavage and processing were successfully replicated in reconstituted vesicles.

    Conclusions:

    • Cleaved signal peptides are not inert but are actively processed within the cell.
    • The endoplasmic reticulum membrane and associated factors play a role in signal peptide processing.
    • The release of processed signal peptides into the cytosol suggests potential downstream functions or degradation pathways.