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Updated: Jul 15, 2026

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
Published on: July 25, 2019
Ubiquitin and ubiquitin-like proteins in protein regulation
Joerg Herrmann1, Lilach O Lerman, Amir Lerman
1Division of Cardiovascular Diseases, Mayo Clinic Rochester, Rochester, MN 55905, USA.
Abstract:
The discovery of the ubiquitin system was awarded with the Nobel Prize in Chemistry in 2004. Labeling of intracellular proteins for degradation by a multienzymatic complex, called the proteasome, was identified as the main function of this system. Subsequently, it was discovered that the attachment of ubiquitin to proteins can modify their function without degradation. Finally, a number of other molecules were recognized to be conjugated to proteins in a manner similar to ubiquitin and were henceforth called ubiquitin-like proteins. This review provides an overview of this class of molecules and its implication for function, subcellular location, and half-life of proteins.
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