HSF and Msn2/4p can exclusively or cooperatively activate the yeast <i>HSP104</i> gene

Grably, Melanie R.; Stanhill, Ariel; Tell, Osnat; Engelberg, David

doi:10.1046/j.1365-2958.2002.02860.x

Cited by 54 publications

(62 citation statements)

References 63 publications

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“…2kbProOsClpB-cyt::Gus rice seedlings in this study showed expression of Gus in response to treatment with Co, Cd, and As. In yeast, Grably et al (2002) noted that the appropriate transcription of Hsp104 is usually obtained through cooperation between the Msn2/4/STRE and the Hsf/ HSE systems and that each factor could activate the promoter alone, backing up the other. Fine mapping of the elements underlying the response to heat and metals in the OsClpB-cyt promoter remains to be carried out.…”

Section: Discussionmentioning

confidence: 99%

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OsHsfA2c and OsHsfB4b are involved in the transcriptional regulation of cytoplasmic OsClpB (Hsp100) gene in rice (Oryza sativa L.)

Singh

Mittal

Lavania

et al. 2012

Cell Stress and Chaperones

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ClpB-cytoplasmic (ClpB-cyt)/Hsp100 is an important chaperone protein in rice. Cellular expression of OsClpB-cyt transcript is governed by heat stress, metal stress, and developmental cues. Transgenic rice plants produced with 2 kb OsClpB-cyt promoter driving Gus reporter gene showed heat-and metal-regulated Gus expression in vegetative tissues and constitutive Gus expression in calli, flowering tissues, and embryonal half of seeds. Rice seedlings regenerated with OsClpB-cyt promoter fragment with deletion of its canonical heat shock element sequence (HSE −273 to −280 ) showed not only heat shock inducibility of Gus transcript/protein but also constitutive expression of Gus in vegetative tissues. It thus emerges that the only classical HSE present in OsClpB-cyt promoter is involved in repressing expression of OsClpB-cyt transcript under unstressed control conditions. Yeast onehybrid assays suggested that OsHsfA2c specifically interacts with OsClpB-cyt promoter. OsHsfA2c also showed binding with OsClpB-cyt and OsHsfB4b showed binding with OsClpB-cyt; notably, interaction of OsHsfB4b was seen for all three OsClpB/Hsp100 protein isoforms (i.e., ClpBcytoplasmic, ClpB-mitochondrial, and ClpB-chloroplastic).Furthermore, OsHsfB4b showed interaction with OsHsfA2c. This study suggests that OsHsfA2c may play a role as transcriptional activator and that OsHsfB4b is an important part of this heat shock responsive circuitry.

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Section: Discussionmentioning

confidence: 99%

“…Apart from HSEs, metal stress responsive elements (STREs) are present in HS promoters. STREs are shown to be important in recruiting metal toxicity specific transcription factors such as MTF-1 in yeast (Grably et al 2002).…”

Section: Noted That the Induced Response To Hs Is Lost If The Canonicmentioning

confidence: 99%

OsHsfA2c and OsHsfB4b are involved in the transcriptional regulation of cytoplasmic OsClpB (Hsp100) gene in rice (Oryza sativa L.)

Singh

Mittal

Lavania

et al. 2012

Cell Stress and Chaperones

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“…Recently, Grably et al (41) reported that transcriptional control of HSP104 is achieved exclusively or cooperatively through activation of heat shock elements and stress response elements. So, we examined the effect of GTS1 gene dosage on the transcription of HSP104 and other genes tested above in response to heat shock.…”

Section: Effect Of Gts1p On Transcription Of Genes Of Hsps and Trehalmentioning

confidence: 99%

“…Gts1p tagged with His 6 at the carboxyl terminus was overexpressed in yeast, and the purified protein was named Gts1p-His 6 . DNA fragments of the upstream sequence of HPS104 ranging from Ϫ271 to Ϫ1 (probe 1) and from Ϫ380 to Ϫ192 (probe 2), with respect to the A of the initiation codon of HSP104, were used as probes, because Grably et al (41) reported that a 334-bp fragment upstream of the first coding AUG is sufficient and essential for maximal basal activity. We tested the gel-shift assay under various binding conditions and found that neither probe formed any complexes with Gts1p-His 6 except for a faint signal that was also found for His 6 as a control (Fig.…”

Section: Fig 8 Subcellular Localization and The Protein Level Of Gtmentioning

confidence: 99%

Gts1p Activates SNF1-dependent Derepression of HSP104 and TPS1 in the Stationary Phase of Yeast Growth

Yaguchi

Tsurugi

2003

Journal of Biological Chemistry

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We previously reported that the GTS1 product, Gts1p, plays an important role in the regulation of heat tolerance of yeast under glucose-limited conditions in either batch or continuous culture. Here we show that heat tolerance was decreased in GTS1-deleted and increased in GTS1-overexpressing cells under glucose-derepressed conditions during the batch culture and that the disruption of SNF1, a transcriptional activator of glucose-repressible genes, diminished this effect of GTS1. Intracellular levels of Hsp104 and trehalose, which were reportedly required for the acquisition of heat tolerance in the stationary phase of cell growth, were affected in both GTS1 mutants roughly in proportion to the gene dosage of GTS1, whereas those of other Hsps were less affected. The mRNA levels of genes for Hsp104 and trehalose-6-phosphate synthase 1 changed as a function of GTS1 gene dosage. The Q-rich domain of Gts1p fused with the DNA-binding domain of LexA activated the transcription of the reporter gene LacZ, and Gts1p lacking the Q-rich domain lost the activation activity of HSP104 and TPS1. Furthermore, Gts1p bound to subunits of Snf1 kinase, whereas it did not bind to DNA. Therefore, we suggested that GTS1 increases heat tolerance by mainly activating Snf1 kinase-dependent derepression of HSP104 and TPS1 in the stationary phase of yeast growth.We reported that the GTS1 gene shows pleiotropic effects on yeast in batch cultures, including the effect on heat tolerance as a function of gene dosage (1); overexpression of GTS1 increases and deletion of GTS1 decreases the heat tolerance of yeast in the stationary phase of growth, whereas no such effects were found in exponentially growing cells. Independently, Bossier et al. (2) isolated GTS1 from cDNA library-transformed yeast which re-grow after lethal heat shock and found that overexpression of GTS1 results in an unchanged growth rate at 37°C compared with 28°C. On the other hand, we reported that GTS1 is involved in regulating ultradian oscillations of energy metabolism in continuous cultures under aerobic and glucose-limited conditions and in the coupling of oscillations of cellular responses to various stress conditions, including heat with the energy metabolism oscillation (3-5). These results suggested that the gene product Gts1p plays an important role in the regulation of heat and other stress responses under glucose-limited or -depleted conditions in either batch or continuous culture.

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“…tially among different heat-shock genes, causing Hsf1p HSF activity must be tightly controlled to avoid inapand Msn2p/4p to have distinct contributions to the propriate expression of heat-shock proteins (Nollen heat-induced expression of these genes (Treger et al and Morimoto 2002). Thus, HSF is negatively regu-1998; Boy- Marcotte et al 1999; Amoros and Estruch lated, kept in an inactive or low activity conformation 2001; Grably et al 2002).…”

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confidence: 99%

Protein Kinase A Regulates Constitutive Expression of Small Heat-Shock Genes in an Msn2/4p-Independent and Hsf1p-Dependent Manner in Saccharomyces cerevisiae

et al. 2005

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Hsf1p, the heat-shock transcription factor from Saccharomyces cerevisiae, has a low level of constitutive transcriptional activity and is kept in this state through negative regulation. In an effort to understand this negative regulation, we developed a novel genetic selection that detects altered expression from the HSP26 promoter. Using this reporter strain, we identified mutations and dosage compensators in the Ras/ cAMP signaling pathway that decrease cAMP levels and increase expression from the HSP26 promoter. In yeast, low cAMP levels reduce the catalytic activity of the cAMP-dependent kinase PKA. Previous studies had proposed that the stress response transcription factors Msn2p/4p, but not Hsf1p, are repressed by PKA. However, we found that reduction or elimination of PKA activity strongly derepresses transcription of the small heat-shock genes HSP26 and HSP12, even in the absence of MSN2/4. In a strain deleted for MSN2/4 and the PKA catalytic subunits, expression of HSP12 and HSP26 depends on HSF1 expression. Our findings indicate that Hsf1p functions downstream of PKA and suggest that PKA might be involved in negative regulation of Hsf1p activity. These results represent a major change in our understanding of how PKA signaling influences the heat-shock response and heat-shock protein expression.

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HSF and Msn2/4p can exclusively or cooperatively activate the yeast HSP104 gene

Cited by 54 publications

References 63 publications

OsHsfA2c and OsHsfB4b are involved in the transcriptional regulation of cytoplasmic OsClpB (Hsp100) gene in rice (Oryza sativa L.)

OsHsfA2c and OsHsfB4b are involved in the transcriptional regulation of cytoplasmic OsClpB (Hsp100) gene in rice (Oryza sativa L.)

Gts1p Activates SNF1-dependent Derepression of HSP104 and TPS1 in the Stationary Phase of Yeast Growth

Protein Kinase A Regulates Constitutive Expression of Small Heat-Shock Genes in an Msn2/4p-Independent and Hsf1p-Dependent Manner in Saccharomyces cerevisiae

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