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Related Experiment Videos

Systematic analysis of stop-transfer sequence for microsomal membrane.

T Kuroiwa1, M Sakaguchi, K Mihara

  • 1Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka, Japan.

The Journal of Biological Chemistry
|May 15, 1991
PubMed
Summary

Investigating protein translocation, this study reveals hydrophobic stretch length and charge influence stop-transfer sequences. Positively charged residues enhance interruption of protein movement across membranes.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Co-translational protein translocation across the endoplasmic reticulum membrane is crucial for protein folding and function.
  • Specific amino acid sequences, termed stop-transfer sequences, can interrupt this process.
  • Understanding the structural requirements of stop-transfer sequences provides insights into the protein translocation machinery.

Purpose of the Study:

  • To systematically examine the structural requirements for stop-transfer sequences.
  • To elucidate the role of hydrophobicity, length, and flanking charged residues in stop-transfer efficiency.
  • To gain information about the protein translocation process through analyzing stop-transfer mechanisms.

Main Methods:

  • Manipulation of interleukin 2 cDNA to insert systematically constructed hydrophobic stretches.

Related Experiment Videos

  • In vitro transcription-translation system using dog pancreas rough microsomes.
  • Analysis of protein topology in the membrane via proteinase K digestion.

    • Main Results:

    • Stop-translocation efficiency is dependent on the hydrophobicity and length of the inserted hydrophobic stretch.
    • Positively charged residues following hydrophobic stretches more effectively interrupted translocation than negatively charged residues.
    • Over 19 alanine residues were needed for efficient stop-translocation, while only 9 leucine residues sufficed.

    Conclusions:

    • Hydrophobic stretch characteristics significantly influence stop-transfer sequence function.
    • Positively charged residues flanking hydrophobic stretches appear to promote stop-translocation.
    • This study provides key structural insights into the mechanisms governing protein translocation across the endoplasmic reticulum membrane.