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Phospholipase C is required for histone acetylation in Saccharomyces cerevisiae
Author(s) -
Galdieri Luciano,
Vancura Ales
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.833.10
Subject(s) - acetylation , histone , histone acetyltransferase , histone deacetylase , histone h2a , microbiology and biotechnology , saccharomyces cerevisiae , chemistry , biology , biochemistry , gene
Phospholipase C (Plc1p) is required for the initial step of inositol polyphosphates (InsPs) synthesis and yeast cells with deletion of PLC1 gene are completely devoid of any InsPs and display aberrations in transcriptional regulation. To address the mechanism how InsPs affect transcriptional regulation, we have utilized inducible FLR1 promoter, which depends on Plc1p for activation. We show that Plc1p is required for normal level of histone H3 acetylation, recruitment of Swi/Snf and SAGA complexes, and nucleosome eviction in the FLR1 promoter. In addition, plc1Δ cells display decreased cellular levels of acetylated histones H3, H4, and histone H2A variant Htz1p. In accordance with the role of Plc1p in supporting histone acetylation, plc1Δ mutation is synthetically lethal with mutations in several subunits of SAGA and NuA4 histone acetyltransferase complexes. Moreover, the growth rate, sensitivity to multiple stresses, and the transcriptional defects of plc1Δ cells are partially suppressed by deletion of histone deacetylase HDA1 . The results thus provide evidence that Plc1p and InsPs are important for normal level of histone acetylation and that InsPs deprivation results in histone hypoacetylation that negatively affects number of physiological processes in plc1Δ cells.