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Nedd8 processing enzymes in Schizosaccharomyces pombe.

ABSTRACT:

Background

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.

Results

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.

Conclusions

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

SUBMITTER: O'Donoghue JE

PROVIDER: S-EPMC3602023 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature

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Nedd8 processing enzymes in Schizosaccharomyces pombe.

O'Donoghue Jean E JE Bech-Otschir Dawadschargal D Larsen Ida B IB Wallace Mairi M Hartmann-Petersen Rasmus R Gordon Colin C

BMC biochemistry 20130315

<h4>Background</h4>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.<h4>Results</h4>Here we show that in the fission ...[more]

PMID: 23496905

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