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Related Experiment Videos

Sequences beyond the cleavage site influence signal peptide function.

D W Andrews1, E Perara, C Lesser

  • 1Department of Physiology, University of California, San Francisco 94143-0444.

The Journal of Biological Chemistry
|October 25, 1988
PubMed
Summary

Signal sequences mediate protein translocation across the endoplasmic reticulum. Deletions in the passenger domain impact translocation efficiency by altering signal-receptor interactions.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Protein secretion is a fundamental cellular process.
  • Targeting and translocation across the endoplasmic reticulum (ER) membrane are critical early steps.
  • Signal sequences direct proteins to the ER.

Purpose of the Study:

  • To investigate how signal sequences mediate protein translocation across the ER membrane in eukaryotes.
  • To understand the role of the translocated protein domain in the efficiency of this process.

Main Methods:

  • Utilizing cell-free systems to study the behavior of fusion proteins and deletion mutants.
  • Analyzing the impact of deletions in the mature prolactin passenger domain on signal sequence function.
  • Examining alterations in interactions with the signal recognition particle (SRP) and signal peptidase.

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Main Results:

  • The protein domain being translocated significantly affects translocation efficiency.
  • Deletions beyond the signal cleavage site in the prolactin passenger domain reduce signal function efficiency.
  • These effects were observed with the signal sequence in its native position and when internalized.

Conclusions:

  • Sequences beyond the signal cleavage site can modulate co-translational translocation efficiency.
  • Changes in these sequences affect interactions with key translocation machinery components like SRP and signal peptidase.
  • This highlights the intricate interplay between signal sequences and their receptors.