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Related Experiment Videos

Membrane protein spanning segments as export signals.

J Calamia1, C Manoil

  • 1Department of Genetics, SK-50, University of Washington, Seattle 98195.

Journal of Molecular Biology
|April 5, 1992
PubMed
Summary
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Escherichia coli lac permease uses specific protein segments to export attached proteins. Efficient export, however, may require interactions between these membrane-spanning segments.

Area of Science:

  • Molecular biology
  • Membrane protein biogenesis
  • Protein translocation

Background:

  • Escherichia coli lac permease is a polytopic integral membrane protein.
  • It possesses six translocated (periplasmic) domains.
  • N-terminal cytoplasmic regions and adjacent membrane-spanning segments act as export signals.

Purpose of the Study:

  • To investigate the role of individual membrane-spanning segments and periplasmic domains in protein export.
  • To identify factors limiting the efficiency of protein translocation across the membrane.

Main Methods:

  • Utilized alkaline phosphatase as a sensor protein attached to different domains of E. coli lac permease.
  • Analyzed the export activity of individual N-terminal cytoplasmic regions and membrane-spanning segments.

Related Experiment Videos

  • Investigated the effect of specific charged residues, such as Arg302, on export efficiency.

    • Main Results:

    • Individual N-terminal cytoplasmic regions and membrane-spanning segments demonstrated export activity for the sensor protein.
    • One specific membrane-spanning segment exhibited significantly lower export activity compared to others.
    • The presence of a positively charged residue (Arg302) was identified as a limiting factor for the export activity of this segment.

    Conclusions:

    • The findings support models where hydrophilic domains are translocated independently during membrane protein insertion.
    • Efficient protein translocation may necessitate cooperative interactions between individual membrane-spanning segments.
    • Specific charged residues can modulate the efficiency of membrane protein export signals.