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Related Experiment Videos

Mutations eliminating the protein export function of a membrane-spanning sequence

E Lee1, C Manoil

  • 1Department of Genetics, University of Washington, Seattle 98195.

The Journal of Biological Chemistry
|November 18, 1994
PubMed
Summary
This summary is machine-generated.

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Specific sequences in membrane proteins are essential for their export. Our study found that pairs of charged amino acids disrupt this process, suggesting a minimum hydrophobicity threshold is required for protein export.

Area of Science:

  • Molecular Biology
  • Protein Biochemistry
  • Membrane Protein Trafficking

Background:

  • Membrane proteins require specific sequences for export from the cell.
  • The first transmembrane domain (TM1) of the Escherichia coli serine chemoreceptor plays a role in protein export.

Purpose of the Study:

  • To identify sequence features within TM1 necessary for protein export.
  • To understand how mutations affect the export function of TM1.

Main Methods:

  • Generated and characterized mutations in the TM1 sequence of the E. coli serine chemoreceptor.
  • Utilized beta-galactosidase and alkaline phosphatase gene fusions to assess protein export function.

Main Results:

  • The export function of TM1 tolerated single charged residues.

Related Experiment Videos

  • Introduction of pairs of charged amino acids was required to abolish export.
  • A model was proposed where export depends on a stretch of uncharged residues exceeding a hydrophobicity threshold.

    • Conclusions:

    • Protein export mediated by TM1 is sensitive to the introduction of charged amino acid pairs.
    • A minimum hydrophobicity threshold for uncharged residues is critical for efficient protein export.
    • This threshold is comparable to that for signal sequence function and observed in wild-type membrane proteins.