PRT6/At5g02310 encodes an Arabidopsis ubiquitin ligase of the N-end rule pathway with arginine specificity and is not the CER3 locus
- 作者：Marcus Garzó ; n ; Karolin Eifler ; Andrea Faust ; Hartmut Scheel ; Kay Hofmann ; Csaba Koncz ; Alex ; er Yephremov ; Andreas Bachmair
- 关键词：CER3 ; N-end rule ; Ubiquitin ; Wax biosynthesis ; Arabidopsis
- 刊名：FEBS Letters
- 出版年：2007
- 期刊代码：70_00145793
- 类别：bio
- 出版时间：10 July 2007
- 卷：581
- 期：17
- 页码：3189-3196
- 文件大小：442 K
摘要
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.