PRT6/At5g02310 encodes an Arabidopsis ubiquitin ligase of the N-end rule pathway with arginine specificity and is not the CER3 locus

FEBS Lett. 2007 Jul 10;581(17):3189-96. doi: 10.1016/j.febslet.2007.06.005. Epub 2007 Jun 12.


The eukaryotic N-end rule pathway mediates ubiquitin- and proteasome-dependent turnover of proteins with a bulky amino-terminal residue. Arabidopsis locus At5g02310 shows significant similarity to the yeast N-end rule ligase Ubr1. We demonstrate that At5g02310 is a ubiquitin ligase and mediates degradation of proteins with amino-terminal Arg residue. Unlike Ubr1, the Arabidopsis protein does not participate in degradation of proteins with amino-terminal Phe or Leu. This modified target specificity coincides with characteristic differences in domain structure. In contrast to previous publications, our data indicate that At5g02310 is not identical to CER3, a gene involved in establishment of a protective surface wax layer. At5g02310 has therefore been re-designated PROTEOLYSIS 6 (PRT6), in accordance with its ubiquitin ligase function.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arabidopsis / genetics
  • Arabidopsis / metabolism
  • Arabidopsis Proteins / genetics*
  • Arabidopsis Proteins / metabolism*
  • Arginine / metabolism*
  • Carbon-Carbon Lyases
  • Models, Biological
  • Nuclear Proteins / genetics*
  • Plants, Genetically Modified
  • Protein Processing, Post-Translational
  • Sequence Analysis, Protein
  • Signal Transduction
  • Substrate Specificity
  • Ubiquitin-Protein Ligases / genetics*
  • Ubiquitin-Protein Ligases / metabolism*


  • Arabidopsis Proteins
  • Nuclear Proteins
  • Arginine
  • PRT6 protein, Arabidopsis
  • Ubiquitin-Protein Ligases
  • CER3 protein, Arabidopsis
  • Carbon-Carbon Lyases