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Identification of genes up-regulated by the overexpression of HSF1 in human HeLa cells

ABSTRACT: To analyze target genes of human heat shock transcription factor 1 (HSF1), we first generated two independent HeLa clones (RDT1 and RDT2) expressing an actively mutated hHSF1 (hHSF1?RDT), which lacks the regulatory domain that masks its activation domain and possesses a glutamic acid at amino acid 395 instead of a leucine in the suppression domain of the trimerization domain (Fujimoto et al., J. Biol. Chem. 280, 34908-34916, 2005). We also generated a HeLa clone expressing chicken HSF1 (HeLa/cHSF1) to compare its profile of gene expression with those of RDT1 and RDT2 cells (Nakai and Morimoto, Mol. Cell. Biol. 13, 1983-1997, 1993). We then carried out DNA microarray analysis using total RNA isolated from HeLa, HeLa/cHSF1, RDT1, and RDT2 cells grown under normal growth conditions. mRNA levels in human HeLa, RDT1, RDT2, and HeLa/cHSF1 were analyzed by DNA microarray analysis using GeneChip Human Genome U133 Plus 2.0 Array (Affymetrix).

ORGANISM(S): Homo sapiens

SUBMITTER: Akira Nakai 

PROVIDER: E-GEOD-19797 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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Publications

Heat shock factor 1 ameliorates proteotoxicity in cooperation with the transcription factor NFAT.

Hayashida Naoki N   Fujimoto Mitsuaki M   Tan Ke K   Prakasam Ramachandran R   Shinkawa Toyohide T   Li Liangping L   Ichikawa Hitoshi H   Takii Ryosuke R   Nakai Akira A  

The EMBO journal 20100910 20

Heat shock transcription factor 1 (HSF1) is an important regulator of protein homeostasis (proteostasis) by controlling the expression of major heat shock proteins (Hsps) that facilitate protein folding. However, it is unclear whether other proteostasis pathways are mediated by HSF1. Here, we identified novel targets of HSF1 in mammalian cells, which suppress the aggregation of polyglutamine (polyQ) protein. Among them, we show that one of the nuclear factor of activated T cells (NFAT) proteins,  ...[more]

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