Abstract
There are a number of known ubiquitin (Ub) derivatives for which hydrolase activities are required to regenerate a functional Ub molecule. For example, removal of ubiquitin from ubiquitinated histones is extensive during metaphase and during periods of altered gene expression. One may expect that Ub, which is a very old protein in evolutionary terms, may be involved in post-translational modifications of other proteins, and hydrolases, possibly with allosteric control features, will be needed to control the degree of modification. Moreover, judging from the gene and mRNA structures that have been reported, some translated forms of Ub will consist of tandem repeats. This calls for Ub-specific peptidases in contrast to the hydrolases introduced above. In fact, fusion proteins involving Ub are rapidly hydrolyzed in yeast. In addition, a variety of conjugates of Ub can arise by reactions of Ub thiol esters of E1 and E2 with the simple thiols and amines that occur in cells. Hydrolysis is the only known way to repair these apparent mistakes.
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Abbreviations
- E1:
-
ubiquitin activating enzyme
- E2:
-
ubiquitin transfer protein
- E3:
-
E2-protein ubiquitin transferase
- Ub:
-
ubiquitin
- Ubal:
-
ubiquitin C-terminal aldehyde
- DTT:
-
dithiothreitol
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© 1988 Springer Science+Business Media New York
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Rose, I.A. (1988). Ubiquitin Carboxyl-Terminal Hydrolases. In: Rechsteiner, M. (eds) Ubiquitin. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-2049-2_6
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DOI: https://doi.org/10.1007/978-1-4899-2049-2_6
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