Nedd8 processing enzymes in Schizosaccharomyces pombe

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• 作者：Jean E O’Donoghue (1)
  Dawadschargal Bech-Otschir (1)
  Ida B Larsen (2)
  Mairi Wallace (1)
  Rasmus Hartmann-Petersen (2)
  Colin Gordon (1)
  
• 关键词：Ubiquitin ; Nedd8 ; Rub1 ; Cullin ; Protein degradation ; Precursor processing
• 刊名：BMC Biochemistry
• 出版年：2013
• 出版时间：December 2013
• 年：2013
• 卷：14
• 期：1
• 全文大小：314KB
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• 作者单位：Jean E O’Donoghue (1)
  Dawadschargal Bech-Otschir (1)
  Ida B Larsen (2)
  Mairi Wallace (1)
  Rasmus Hartmann-Petersen (2)
  Colin Gordon (1)
  
  1. MRC Human Genetics Unit, Western General Hospital, Crewe Road, Edinburgh, EH4 2XU, UK
  2. Department of Biology, University of Copenhagen, Ole Maal?es Vej 5, Copenhagen, DK-2200, Denmark
  

文摘

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.