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Purification and Structural Properties of Ubiquitin

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Ubiquitin

Abstract

This chapter discusses the purification and characteristics of ubiquitin (Ub),1 the highly conserved and widely distributed peptide that participates in a variety of cellular functions. As this book makes clear, Ub has a role in protein degradation,2–4 chromatin structure,5–7 the heat-shock response,8,9 cell surface receptors,10–12 and perhaps even immunological response.13 The one unifying theme in all these functions is the formation of an amide bond between the carboxyl terminus of Ub and amino groups of a variety of proteins. Thus, Ub can be thought of as a marker molecule that targets proteins for any of a variety of metabolic fates. One of the critical unanswered questions about its mode of action involves the definition of how Ub contributes to the partition of various Ub-protein conjugates between these metabolic fates.

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Authors and Affiliations

  1. Department of Biochemistry, Emory University School of Medicine, Atlanta, 30322, Georgia

    Keith D. Wilkinson

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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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Wilkinson, K.D. (1988). Purification and Structural Properties of Ubiquitin. In: Rechsteiner, M. (eds) Ubiquitin. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-2049-2_2

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  • DOI: https://doi.org/10.1007/978-1-4899-2049-2_2

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4899-2051-5

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