By Josep M. Argiles

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Ubp3: The gene has been cloned and encodes a 102 kDa protein. The enzyme cleaves ubiquitin-protein fusions. No phenotypic defects have been reported in Ubp3 mutants. Ubp4/Doa4: The gene has been cloned and encodes a 105 kDa protein. Interestingly, this deubiquitinating enzyme is thought to be part of the 26S proteasome, since purified preparations of the yeast 26S proteasome contain the Doa4 protein. The enzyme is believed to work in conjunction with the 26S proteasome, probably in the latter stages of proteolysis.

5 In addition, its activating activity is believed to be needed for almost all known ubiquitin transfers. In fact, the UBA1 protein or its rabbit homolog has been used in many in vitro ubiquitin-transfer assays. Furthermore, the use of temperature-sensitive mutants obtained from possible mammalian homologs of UBA1 has shown that ubiquitin activation is linked to most of the known ubiquitin mediated functions. 77,82,83 Whereas the amino acid sequence of wheat UBA2 is nearly identical to UBA1, the sequence of UBA3 is significantly different.

Either E2F1 or ubcH5 participate in conjunction with this ligase in the processing of the p105 precursor protein. RAD18: This is another protein that binds (it constitutes an E3-like factor) to DNA damaged regions and to the UBC2/ RAD6 enzyme,161 probably acting as an E3-like factor in DNA repair. 30 Two types of activity have been reported in this family of enzymes. One type of activity is able to cleave ubiquitin from small peptides or proteins that may either be biosynthetic precursors of ubiquitin or of small proteins, while the other type cleave ubiquitin from small intracellular nucleophiles, such as amines or glutathion, that would rapidly consume the free ubiquitin pools.

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