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A signal sequence is not sufficient to lead β-galactosidase out of the cytoplasm

Nature volume 286, pages 356–359 (1980)Cite this article

Abstract

Escherichia coli strains have been constructed in which lacZ, the gene for the cytoplasmic enzyme β-galactosidase, is fused to lamB, the gene for an outer membrane protein. One such strain produces a β-galactosidase which remains cytoplasmic even though it possesses the complete signal sequence of the lamB protein precursor at the amino-terminal end.

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Author notes

  1. Felipe Moreno

    Present address: Servicio de Microbiologia, Centro Especial Ramon y Cajal, Madrid, 34, Spain

Authors and Affiliations

  1. Unité de Génétique Moléculaire, Institut Pasteur 25 rue du Dr Roux, 75724, Paris, Cedex 15, France

    Felipe Moreno & Maxime Schwartz

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

    Audree V. Fowler & Irving Zabin

  3. Frederick Cancer Research Center, Cancer Biology Program, Frederick, Maryland, 21701

    Michael Hall & Thomas J. Silhavy

Authors
  1. Felipe Moreno
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  2. Audree V. Fowler
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  3. Michael Hall
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  4. Thomas J. Silhavy
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  5. Irving Zabin
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  6. Maxime Schwartz
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Moreno, F., Fowler, A., Hall, M. et al. A signal sequence is not sufficient to lead β-galactosidase out of the cytoplasm. Nature 286, 356–359 (1980). https://doi.org/10.1038/286356a0

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