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Molecular and General Genetics MGG

, Volume 264, Issue 1–2, pp 64–74 | Cite as

Up-regulation of genes encoding glycosylphosphatidylinositol (GPI)-attached proteins in response to cell wall damage caused by disruption of FKS1 in Saccharomyces cerevisiae

  • H. Terashima
  • N. Yabuki
  • M. Arisawa
  • K. Hamada
  • K. Kitada
Original Paper

Abstract

FKS1 and FKS2 encode alternative catalytic subunits of the glucan synthases that are responsible for synthesis of β-1,3-glucan in the Saccharomyces cerevisiae cell wall. Disruption of FKS1 reduces the glucan content of the cell wall, increases chitin content and activates the expression of CWP1, which encodes a glycosylphosphatidylinositol (GPI)-dependent cell wall protein. These cellular responses have been regarded as compensating for cell wall damage in order to maintain cell wall integrity. Here, we report the identification, by genome-wide screening, of 22 genes that are transcriptionally up-regulated in fks1 Δ cells. Among them, five genes were found to encode GPI-attached proteins, three of which are covalently associated with the cell wall. Deletion and replacement analysis of the promoter regions identified Rlm1-binding sequences as being responsible for the up-regulation following disruption of FKS1. Using the rlm1 Δ tetOp-FKS1 strain, in which the expression of FKS1 can be repressed by doxycycline, we examined the requirement for Rlm1 for the transcriptional up-regulation of these five genes. Three of the five genes were not up-regulated by doxycycline, indicating that Rlm1 mediates their up-regulation when FKS1 is inactivated. The remaining two genes were up-regulated by doxycycline, suggesting that a transcription factor other than Rlm1 is involved in their response to disruption of FKS1.

FKS1 Cell wall damage RLM1 GPI proteins Saccharomyces cerevisiae 

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Copyright information

© Springer-Verlag 2000

Authors and Affiliations

  • H. Terashima
    • 1
  • N. Yabuki
    • 1
  • M. Arisawa
    • 1
  • K. Hamada
    • 1
  • K. Kitada
    • 1
  1. 1.Department of Mycology, Nippon Roche Research Center, 200-Kajiwara, Kamakura, Kanagawa 247-8530Japan

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