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Related Experiment Videos

Many random sequences functionally replace the secretion signal sequence of yeast invertase.

C A Kaiser, D Preuss, P Grisafi

    Science (New York, N.Y.)
    |January 16, 1987
    PubMed
    Summary

    Researchers explored how amino-terminal signal sequences direct protein secretion. They found that about 20% of random sequences can function as export signals, indicating low specificity in signal recognition.

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    Area of Science:

    • Molecular Biology
    • Protein Secretion
    • Yeast Genetics

    Background:

    • Amino-terminal signal sequences are crucial for directing proteins to secretion pathways.
    • The precise relationship between the amino acid sequence of these signals and their export function is not well understood.
    • Understanding signal sequence function is key to controlling protein localization and secretion.

    Purpose of the Study:

    • To determine the permissible sequence variations for functional amino-terminal signal sequences.
    • To investigate the specificity of the cellular machinery that recognizes signal sequences.
    • To elucidate the relationship between primary peptide sequence and protein export efficiency.

    Main Methods:

    • Systematic replacement of the native signal sequence of Saccharomyces cerevisiae invertase with randomized peptide sequences.

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  • Functional assessment of these altered signal sequences in the protein secretion pathway.
  • Analysis of sequence diversity among functional export signals.

    • Main Results:

    • Approximately one-fifth (20%) of the tested random peptide sequences retained the ability to function as export signals.
    • This suggests a broad tolerance for sequence variation within functional signal sequences.
    • The findings challenge the notion of high specificity in signal sequence recognition.

    Conclusions:

    • Signal sequence recognition by the protein secretion machinery exhibits surprisingly low specificity.
    • A wide range of amino acid sequences can effectively mediate protein export.
    • This implies that the structural rather than the precise primary sequence may be more critical for signal function.