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Eukaryotic Cell, June 2008, p. 967-979, Vol. 7, No. 6
1535-9778/08/$08.00+0     doi:10.1128/EC.00438-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Saccharomyces cerevisiae Phospholipase C Regulates Transcription of Msn2p-Dependent Stress-Responsive Genes ^,

Agnieszka Demczuk,^1, Nilanjan Guha,^1,, Peter H. Nguyen,^1,,¶ Parima Desai,^1,|| Jennifer Chang,¹ Katarzyna Guzinska,¹ Janet Rollins,^1,# Chandra C. Ghosh,¹ Leslie Goodwin,² and Ales Vancura^1*

Department of Biological Sciences, St. John's University, Queens, New York 11439,¹ North Shore-Long Island Jewish Research Institute, Manhasset, New York 11030²

Received 30 November 2007/ Accepted 17 March 2008

Phosphatidylinositol phosphates are involved in signal transduction, cytoskeletal organization, and membrane trafficking. Inositol polyphosphates, produced from phosphatidylinositol phosphates by the phospholipase C-dependent pathway, regulate chromatin remodeling. We used genome-wide expression analysis to further investigate the roles of Plc1p (phosphoinositide-specific phospholipase C in Saccharomyces cerevisiae) and inositol polyphosphates in transcriptional regulation. Plc1p contributes to the regulation of approximately 2% of yeast genes in cells grown in rich medium. Most of these genes are induced by nutrient limitation and other environmental stresses and are derepressed in plc1 cells. Surprisingly, genes regulated by Plc1p do not correlate with gene sets regulated by Swi/Snf or RSC chromatin remodeling complexes but show correlation with genes controlled by Msn2p. Our results suggest that the increased expression of stress-responsive genes in plc1 cells is mediated by decreased cyclic AMP synthesis and protein kinase A (PKA)-mediated phosphorylation of Msn2p and increased binding of Msn2p to stress-responsive promoters. Accordingly, plc1 cells display other phenotypes characteristic of cells with decreased PKA activity. Our results are consistent with a model in which Plc1p acts together with the membrane receptor Gpr1p and associated G protein Gpa2p in a pathway separate from Ras1p/Ras2p and converging on PKA.

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* Corresponding author. Mailing address: Department of Biological Sciences, St. John's University, 8000 Utopia Parkway, Queens, NY 11439. Phone: (718) 990-6287. Fax: (718) 990-5958. E-mail: vancuraa{at}stjohns.edu

Published ahead of print on 28 March 2008.

Supplemental material for this article may be found at http://ec.asm.org/.

These authors contributed equally to this work.

Present address: Harvard Medical School, 240 Longwood Ave., Boston, MA 02115.

^¶ Present address: Borough of Manhattan Community College, The City University of New York, 199 Chambers Street, New York, NY 10007.

^|| Present address: University of Massachusetts Medical School, 364 Plantation Street, Worcester, MA 01605.

^# Present address: College of Mount Saint Vincent, 6301 Riverdale Avenue, Riverdale, NY 10471.

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Eukaryotic Cell, June 2008, p. 967-979, Vol. 7, No. 6
1535-9778/08/$08.00+0     doi:10.1128/EC.00438-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.