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Genes to Cells (2006) 11, 59-69. doi:10.1111/j.1365-2443.2005.00921.x
© 2006 Blackwell Publishing or its licensors
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Yeast unfolded protein response pathway regulates expression of genes for anti-oxidative stress and for cell surface proteins

Yukio Kimata*, Yuki Ishiwata-Kimata, Seiko Yamada and Kenji Kohno*

Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan

The unfolded protein response (UPR) is a cellular protective event against endoplasmic reticulum (ER) stress. In the yeast UPR signaling pathway, the ER-located transmembrane protein Ire1 promotes splicing of the HAC1 premRNA (HAC1u) to produce the translatable transcription factor mRNA (HAC1i). We generated a HAC1i gene-bearing strain, in which the UPR pathway was constitutively activated, and compared its gene expression profile with that of a {Delta}ire1 HAC1u strain using cDNA microarray technology. Comparison of the gene expression profile was also performed between non-stressed wild-type cells and those exposed to ER stress. Genes for which the expression level was significantly changed in both of these experiments were categorized as targets of the Ire1-HAC1 signaling pathway. This analysis revealed that in addition to the previously known UPR targets, some anti-oxidative stress genes were up-regulated by the Ire1-HAC1 pathway, possibly in order to reduce reactive oxygen species produced during the cellular response to ER stress. Moreover, we categorized 15 genes as those down-regulated by the UPR, most of which seem to encode cell surface or extracellular proteins. This UPR-mediated gene repression may alleviate the load of client proteins targeted to the ER.

Communicated by: Keiji Tanaka

* Correspondence: E-mail: kimata{at}zero.ad.jp, kimata{at}bs.naist.jp, kkouno{at}bs.naist.jp




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