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Evolution and function of ubiquitin-like protein-conjugation systems

Nature Cell Biology volume 2, pages E153–E157 (2000)Cite this article

An Erratum to this article was published on 01 November 2000

Abstract

Ubiquitin functions by covalently modifying other proteins. In the past few years, a surprising number of other proteins have been identified that, despite often being only slightly similar to ubiquitin, can also be attached to proteins. Newly discovered parallels between the activation of ubiquitin and the biosynthesis of certain enzyme cofactors now hint at the possible evolutionary origins of the ubiquitin system.

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Figure 1: Reversible ligation of ubiquitin and Ubls to other proteins.
Figure 2: The ubiquitin family of protein modifiers.
Figure 3: Sequence similarities between ubiquitin and Ubls.
Figure 4: Potential parallels between sulphurtransferases and Ubl transferases.

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Acknowledgements

I wish to thank J. Laney, S-J. Li, C. Pickart and R. Swanson for helpful discussion and comments on the manuscript. The work of my laboratory is supported by grants from the NIH.

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  1. Department of Molecular Biophysics, Biochemistry Yale University, 266 Whitney Avenue, New Haven, 06520, Connecticut, USA

    Mark Hochstrasser

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Correspondence to Mark Hochstrasser.

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Hochstrasser, M. Evolution and function of ubiquitin-like protein-conjugation systems . Nat Cell Biol 2, E153–E157 (2000). https://doi.org/10.1038/35019643

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