Nedd8 processing enzymes in Schizosaccharomyces pombe

Jean E O'Donoghue1, Dawadschargal Bech-Otschir, Ida B Larsen

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

BMC Biochemistry
|March 19, 2013
PubMed
Abstract

Insights

In fission yeast, Uch1 is not the only enzyme that processes the Nedd8 precursor. Deubiquitylating enzymes also play a key role in Nedd8 activation, which is crucial for SCF ligase function.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • The conjugation of ubiquitin-like modifier Nedd8 to cullins is essential for SCF-type ubiquitin ligase activity.
  • SCF ligases regulate the degradation of various substrates, including cell cycle regulators.
  • Nedd8, like ubiquitin, is synthesized as an inactive precursor requiring processing for activation.

Purpose of the Study:

  • To investigate the enzymes responsible for Nedd8 precursor processing in the fission yeast Schizosaccharomyces pombe.
  • To determine if the Yuh1 orthologue, Uch1, is the sole Nedd8-processing enzyme in S. pombe.

Main Methods:

  • Comparative analysis of Nedd8 processing in Schizosaccharomyces pombe.
  • Identification and characterization of enzymes involved in Nedd8 precursor maturation in vivo.

Main Results:

  • The Yuh1 orthologue, Uch1, is not the exclusive enzyme for Nedd8 precursor processing in S. pombe.
  • Deubiquitylating enzymes were found to efficiently process the Nedd8 precursor in vivo.

Conclusions:

  • Nedd8 precursor processing in S. pombe involves multiple enzymes.
  • A variety of deubiquitylating enzymes contribute to the activation of Nedd8 in vivo.

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