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The glycosylphosphatidylinositol-linked aspartyl protease Yps1 is transcriptionally regulated by the calcineurin-Crz1 and Slt2 MAPK pathways in Candida glabrata.


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Title: The glycosylphosphatidylinositol-linked aspartyl protease Yps1 is transcriptionally regulated by the calcineurin-Crz1 and Slt2 MAPK pathways in Candida glabrata.
Authors: Miyazaki, Taiga / Izumikawa, Koichi / Yamauchi, Shunsuke / Inamine, Tatsuo / Nagayoshi, Yohsuke / Saijo, Tomomi / Seki, Masafumi / Kakeya, Hiroshi / Yamamoto, Yoshihiro / Yanagihara, Katsunori / Miyazaki, Yoshitsugu / Yasuoka, Akira / Kohno, Shigeru
Issue Date: Aug-2011
Publisher: Blackwell Publishing Inc.
Citation: FEMS Yeast Research, 11(5), pp.449-456; 2011
Abstract: In the pathogenic fungus Candida glabrata, the YPS1 gene, which encodes a glycosylphosphatidylinositol-linked aspartyl protease, is required for cell wall integrity and virulence. Although the expression of YPS1 has been studied in Saccharomyces cerevisiae, the transcriptional regulation of this gene in C. glabrata is not well understood. Here, we report that C. glabrata Yps1 is required for cell growth at elevated temperatures, and that the heat-induced expression of YPS1 is regulated predominantly by the calcineurin-Crz1 pathway and partially by the Slt2 MAPK pathway. Although a total of 11 YPS genes are present in the C. glabrata genome, the loss of transcriptional induction in a calcineurin mutant was observed only for YPS1. The results of a YPS1 promoter-lacZ reporter assay using a series of constructs with mutated promoter elements indicated that the transcription factor Crz1 binds to multiple sites in the promoter region of YPS1. To date, as none of the putative Crz1 targets in C. glabrata have been characterized using a Δcrz1 mutant, monitoring the expression of YPS1 represents an effective method for measuring the activity of the calcineurin-Crz1 signaling pathway in this fungus.
Keywords: Cell wall integrity / Mpk1 / Yapsin
URI: http://hdl.handle.net/10069/27426
ISSN: 15671356
DOI: 10.1111/j.1567-1364.2011.00734.x
PubMed ID: 21501380
Rights: © 2011 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved
Type: Journal Article
Text Version: author
Appears in Collections:Articles in academic journal

Citable URI : http://hdl.handle.net/10069/27426

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