Work

Nedd8 processing enzymes in Schizosaccharomyces pombe

Year: 2013

Type: article

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.

Source: BMC Biochemistry

DOI: 10.1186/1471-2091-14-8

Authors: Jean E O’Donoghue, Dawadschargal Bech-Otschir, Ida B Larsen, Mairi Wallace, Rasmus Hartmann-Petersen, Colin Gordon

Institutions: Western General Hospital, MRC Human Genetics Unit, University of Copenhagen

Language: English

Topic: Ubiquitin and proteasome pathways

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $2,170

Funders: Lundbeckfonden, H. Lundbeck A/S, Medical Research Council