PRT6/At5g02310 encodes an Arabidopsis ubiquitin ligase of the N-end rule pathway with arginine specificity and is not the CER3 locus.
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.
Garzón
Marcus
M
Department of Plant Developmental Biology, Max Planck Institute for Plant Breeding Research, Carl-von-Linné-Weg 10, Cologne, Germany.
Eifler
Karolin
K
Faust
Andrea
A
Scheel
Hartmut
H
Hofmann
Kay
K
Koncz
Csaba
C
Yephremov
Alexander
A
Bachmair
Andreas
A
D017360:Arabidopsis / Q000235:genetics / Q000378:metabolism; D029681:Arabidopsis Proteins / Q000235:genetics* / Q000378:metabolism*; D001120:Arginine / Q000378:metabolism*; D019755:Carbon-Carbon Lyases; D008954:Models, Biological; D009687:Nuclear Proteins / Q000235:genetics*; D030821:Plants, Genetically Modified; D011499:Protein Processing, Post-Translational; D020539:Sequence Analysis, Protein; D015398:Signal Transduction; D013379:Substrate Specificity; D044767:Ubiquitin-Protein Ligases / Q000235:genetics* / Q000378:metabolism*
D029681:Arabidopsis Proteins; D001120:Arginine; D019755:Carbon-Carbon Lyases; D009687:Nuclear Proteins; D044767:Ubiquitin-Protein Ligases; C523368:PRT6 protein, Arabidopsis; C103487:At5g57800 protein, Arabidopsis