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Nedd8 processing enzymes in Schizosaccharomyces pombe

Jean E O’Donoghue1, Dawadschargal Bech-Otschir1, Ida B Larsen2, Mairi Wallace1, Rasmus Hartmann-Petersen2 and Colin Gordon1*

Author Affiliations

1 MRC Human Genetics Unit, Western General Hospital, Crewe Road, Edinburgh, EH4 2XU, UK

2 Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, Copenhagen, DK-2200, Denmark

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BMC Biochemistry 2013, 14:8  doi:10.1186/1471-2091-14-8

Published: 15 March 2013



Conjugation of the ubiquitin-like modifier Nedd8 to cullins is critical for the function of SCF-type ubiquitin ligases and thus facilitates ubiquitin conjugation and ultimately degradation of SCF substrates, including several cell cycle regulators. Like ubiquitin, Nedd8 is produced as a precursor that must first be processed before it becomes active. In Saccharomyces cerevisiae this is carried out exclusively by the enzyme Yuh1.


Here we show that in the fission yeast, Schizosaccharomyces pombe, the Yuh1 orthologue, Uch1, is not the sole Nedd8 processing enzyme. Instead it appears that deubiquitylating enzymes can efficiently process the Nedd8 precursor in vivo.


Several enzymes contribute to Nedd8 precursor processing including a number of deubiquitylating enzymes.

Ubiquitin; Nedd8; Rub1; Cullin; Protein degradation; Precursor processing