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PRT6 /At5g02310 encodes an Arabidopsis ubiquitin ligase of the N‐end rule pathway with arginine specificity and is not the CER3 locus
Author(s) -
Garzón Marcus,
Eifler Karolin,
Faust Andrea,
Scheel Hartmut,
Hofmann Kay,
Koncz Csaba,
Yephremov Alexander,
Bachmair Andreas
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.06.005
Subject(s) - ubiquitin ligase , arabidopsis , ubiquitin , dna ligase , biochemistry , proteolysis , biology , locus (genetics) , arginine , amino acid , gene , chemistry , genetics , mutant , enzyme
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.