NDLI: Relationship of DFG16 to the Rim101p pH Response Pathway in Saccharomyces cerevisiae and Candida albicans †

Content Provider	PubMed Central
Author	Barwell, Karen J. Boysen, Jacob H. Xu, Wenjie Mitchell, Aaron P.
Copyright Year	2005
Abstract	Many fungal pH responses depend upon conserved Rim101p/PacC transcription factors, which are activated by C-terminal proteolytic processing. The means by which environmental pH is sensed by this pathway are not known. Here, we report a screen of the Saccharomyces cerevisiae viable deletion mutant library that has yielded a new gene required for processed Rim101p accumulation, DFG16. An S. cerevisiae dfg16Δ mutant expresses Rim101p-repressed genes at elevated levels. In addition, Candida albicans dfg16Δ/dfg16Δ mutants are defective in alkaline pH-induced filamentation, and their defect is suppressed by expression of truncated Rim101-405p. Thus, Dfg16p is a functionally conserved Rim101p pathway member. Many proteins required for processed Rim101p accumulation are members of the ESCRT complex, which functions in the formation of multivesicular bodies (MVBs). Staining with the dye FM4-64 indicates that the S. cerevisiae dfg16Δ mutant does not have an MVB defect. We find that two transcripts, PRY1 and ASN1, respond to mutations that affect both the Rim101p and MVB pathways but not to mutations that affect only one pathway. The S. cerevisiae dfg16Δ mutation does not affect PRY1 and ASN1 expression, thus confirming that Dfg16p function is restricted to the Rim101p pathway. Dfg16p is homologous to Aspergillus nidulans PalH, a component of the well-characterized PacC processing pathway. We verify that the previously recognized PalH homolog, Rim21p, also functions in the S. cerevisiae Rim101p pathway. Dfg16p is predicted to have seven membrane-spanning segments and a long hydrophilic C-terminal region, as expected if Dfg16p were a G-protein-coupled receptor.
Related Links	http://dx.doi.org/10.1128/ec.4.5.890-899.2005
Ending Page	899
Page Count	10
Starting Page	890
File Format	PDF
ISSN	15359778
e-ISSN	15359786
Journal	Eukaryotic Cell
Issue Number	5
Volume Number	4
Language	English
Publisher	American Society for Microbiology
Publisher Date	2005-05-01
Access Restriction	Open
Rights Holder	American Society for Microbiology
Subject Keyword	Molecular Biology Microbiology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Microbiology

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