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Transcriptional activity of a gene is governed by transcriptional regulatory complexes that assemble/disassemble on the gene and control the chromatin architecture. How cytoplasmic components influence the assembly/disassembly of transcriptional regulatory complexes is poorly understood. Here we report that the budding yeast  Saccharomyces cerevisiae  has a chromatin architecture-modulating mechanism that is dependent on the endosomal lipid PI(3,5)P 2 . We identified Tup1 and Cti6 as new, highly specific PI(3,5)P 2  interactors. Tup1—which associates with multiple transcriptional regulators, including the HDAC (histone deacetylase) and SAGA complexes—plays a crucial role in determining an activated or repressed chromatin state of numerous genes, including  GAL1 . We show that, in the context that the Gal4 activation pathway is compromised, PI(3,5)P 2  plays an essential role in converting the Tup1-driven repressed chromatin structure into a SAGA-containing activated chromatin structure at the  GAL1  promoter. Biochemical and cell biological experiments suggest that PI(3,5)P 2  recruits Cti6 and the Cyc8–Tup1 corepressor complex to the late endosomal/vacuolar membrane and mediates the assembly of a Cti6–Cyc8–Tup1 coactivator complex that functions to recruit the SAGA complex to the  GAL1  promoter. Our findings provide important insights toward understanding how the chromatin architecture and epigenetic status of a gene are regulated by cytoplasmic components.

Phosphoinositide [PI(3,5)P2] lipid-dependent regulation of the general transcriptional regulator Tup1

Phosphoinositide [PI(3,5)P₂] lipid-dependent regulation of the general transcriptional regulator Tup1