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Mutations which alter the function of the signal sequence of the maltose binding protein of Escherichia coli

Nature volume 285, pages 78–81 (1980)Cite this article

Abstract

The maltose binding protein of Escherichia coli is secreted into the external periplasmic compartment of the cell by virtue of an amino-terminal signal sequence. Using DNA sequencing, we have determined the precise nature of mutations in the signal sequence which prevent the export of the maltose binding protein, causing it to accumulate in the cytoplasm in its precursor form. In most cases, the change of a single hydrophobic or uncharged amino acid to a charged amino acid within the signal sequence is sufficient to block the secretion process.

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Author information

Authors and Affiliations

  1. Unité de Génie Génétique, Institut Pasteur, 75015, Paris, France

    Huges Bedouelle & Maurice Hofnung

  2. Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts, 02115

    Philip J. Bassford Jr & Jon Beckwith

  3. Department of Biological Chemistry, UCLA School of Medicine and Molecular Biology Institute, University of California, Los Angeles, California, 90024

    Audree V. Fowler & Irving Zabin

Authors
  1. Huges Bedouelle
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  2. Philip J. Bassford Jr
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  3. Audree V. Fowler
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  4. Irving Zabin
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  5. Jon Beckwith
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  6. Maurice Hofnung
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Bedouelle, H., Bassford, P., Fowler, A. et al. Mutations which alter the function of the signal sequence of the maltose binding protein of Escherichia coli. Nature 285, 78–81 (1980). https://doi.org/10.1038/285078a0

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