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Protein Breakdown and the Heat-Shock Response

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Abstract

A primary function of protein breakdown in animal and bacterial cells is to eliminate nonfunctional or denatured polypeptides whose accumulation in vivo could be quite toxic.1–4 Proteins with highly abnormal structures may result from nonsense mutations, insertions or deletions, missense mutations, biosynthetic errors, incorporation of amino acid analogs into proteins, or postsynthetic damage to normal cell constituents. However, such polypeptides generally fail to accumulate in vivo to the levels of normal gene products because they are rapidly degraded to amino acids.

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  1. Stephen A. Goff

    Present address: U.S. Department of Agriculture, Plant Gene Expression Center, Albany, California, 94710, USA

Authors and Affiliations

  1. Department of Physiology, Tufts Medical School, Boston, Massachusetts, 02111, USA

    Stephen A. Goff

  2. Department of Biochemistry and Molecular Biology, University of Miami School of Medicine, Miami, Florida, 33136, USA

    Richard Voellmy

  3. Department of Physiology and Biophysics, Harvard Medical School, Boston, Massachusetts, 02115, USA

    Alfred L. Goldberg

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  1. Department of Biochemistry, School of Medicine, University of Utah, Salt Lake City, Utah, 84132, USA

    Martin Rechsteiner

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Goff, S.A., Voellmy, R., Goldberg, A.L. (1988). Protein Breakdown and the Heat-Shock Response. In: Rechsteiner, M. (eds) Ubiquitin. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-2049-2_9

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