Authors: Lingzhu Wei Ye Tao Haiyan Jia Lixia Zhang Pei Xu Yuezhi Wang Zhengzhi Zhang Caiqin Zhang Zhengqiang Ma
Publish Date: 2009/05/30
Volume: 27, Issue: 4, Pages: 439-447
Abstract
The UFD1 protein is an important ubiquitin recognition component in the ubiquitinmediated degradation pathway To investigate the conservation of UFD1 genes among eukaryotes and their differentiation two UFD1 paralogs from wheat were identified and mapped to homoeologous chromosome groups 6 and 2 respectively TaUFD1a6B and TaUFD1b2D were cloned and both genes consist of eight introns and of the same intron phases These genes were compared with those in Arabidopsis rice polar yeast and mammals for their sequence chromosome organization and primary protein structure The sequence structure especially those corresponding to the fourth fifth and sixth exons of UFD1 genes is highly conserved across these taxa However unlike yeast and mammals having a single UFD1 gene higher angiosperm species have two ancient UFD1 paralogs Besides the evolutionarily conserved ubiquitinbinding domain at the Nterminus plant UFD1 proteins have three conserved Cterminal motifs Motif I near the UFD1 domain displays a high level of similarity to the mammalian p97binding site and motif III is likely responsible for endoplasmic reticulum membrane retention TaUFD1a6B and TaUFD1b2D are ubiquitously expressed in different plant tissues A green fluorescent proteintransient expression assay in epidermal cells of onion demonstrated that TaUFD1 proteins primarily accumulate in the nucleus
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