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Direct Demonstration of Cotranslational Secretion of Proteins in Bacteria

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Membranes and Transport

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Abstract

In animal cells a special role for the ribosomes bound to the endoplasmic reticulum was recognized early by Palade and co-workers (reviewed in Palade, 1975), who observed a parallel between the abundance of such ribosomes and the secretion of proteins. Various secretory proteins were shortly shown to be synthesized on the membrane-bound polysomes, and various cytoplasmic proteins on the free polysomes (reviewed in Rollerston, 1974). This distribution suggested that secreted proteins might cross the membrane as growing chains, rather than after completion. In support of this model, Redman and Sabatini (1966) found that puromycin released incomplete chains to the interior of the microsomes.

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Authors and Affiliations

  1. Bacterial Physiology Unit, Harvard Medical School, Boston, Massachusetts, 02115, USA

    Phang-C. Tai & Bernard D. Davis

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  1. Phang-C. Tai
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  2. Bernard D. Davis
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Editors and Affiliations

  1. Department of Biochemistry, State University of New York, Upstate Medical Center, 13210, Syracuse, New York, USA

    Anthony N. Martonosi

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© 1982 Plenum Press, New York

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Tai, PC., Davis, B.D. (1982). Direct Demonstration of Cotranslational Secretion of Proteins in Bacteria. In: Martonosi, A.N. (eds) Membranes and Transport. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-4082-9_38

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  • DOI: https://doi.org/10.1007/978-1-4684-4082-9_38

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-4084-3

  • Online ISBN: 978-1-4684-4082-9

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