Characterization of two homologs of Ire1p, a kinase/endoribonuclease in yeast, in Arabidopsis thaliana

被引：62

作者：

Noh, SJ ^{[1
]}

Kwon, CS ^{[1
]}

Chung, WI ^{[1
]}

机构：

[1] Korea Adv Inst Sci & Technol, Dept Biol Sci, Yusong Gu, Taejon 305701, South Korea

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION | 2002年 / 1575卷 / 1-3期

关键词：

IRE1; kinase/endoribonuclease; unfolded protein response; endoplasmic reticulum stress;

D O I：

10.1016/S0167-4781(02)00237-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The accumulation of unfolded proteins in the endoplasmic reticulum (ER) elicits an ER-to-nucleus signaling pathway known as the unfolded protein response (UPR) in eukaryotes. In yeast, Ire1p, a kinase/endoribonuclease in the ER membrane, plays a key role in the UPR signaling. We isolated two cDNA homologs of IRE1 gene from Arabidopsis (AtIre1a, AtIre1b). The two IRE1 homologs were predicted to form a type I transmembrane protein structure and contain kinase/endoribonuclease domains at their C-terminal halves. The expressions of the two genes were detected in various organ tissues of the Arabidopsis plant. The C-terminal half of the AtIre1a protein showed in vitro autophosphorylation activity. However, we could not detect endoribonuclease activity of the AtIre1a protein when we used yeast HAC1 RNA as the substrate in vivo. (C) 2002 Elsevier Science B.V. All rights reserved.

引用

页码：130 / 134

页数：5

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