Oxidative stress induced heat shock factor phosphorylation and HSF-dependent activation of yeast metallothionein gene transcription.

Liu, Xiaodong; Thiele, Dennis J.

doi:10.1101/gad.10.5.592

Cited by 150 publications

(166 citation statements)

References 58 publications

(87 reference statements)

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“…Human IL1␤ is repressed by heat shock, and yeast CUP1 is induced by oxidative stress under conditions that have little effect on hsp70. CUP1 expression appears to correlate with phosphorylation at sites different from those that are phosphorylated during heat shock (Liu and Thiele, 1996). These differences in HSF function appear to be determined in part by the nature of the HSF-binding site (Santoro et al, 1998).…”

Section: Discussionmentioning

confidence: 96%

“…This possibility is especially significant when viewed in combination with the findings of Liu and Thiele (1996) and Cahill et al (1996) that there are genes that are regulated by HSF in distinctly different ways than the traditional heat shock genes. Human IL1␤ is repressed by heat shock, and yeast CUP1 is induced by oxidative stress under conditions that have little effect on hsp70.…”

Section: Discussionmentioning

confidence: 98%

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Complex Regulation of the Yeast Heat Shock Transcription Factor

Bonner

Carlson

Fackenthal

et al. 2000

MBoC

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The yeast heat shock transcription factor (HSF) is regulated by posttranslational modification. Heat and superoxide can induce the conformational change associated with the heat shock response. Interaction between HSF and the chaperone hsp70 is also thought to play a role in HSF regulation. Here, we show that the Ssb1/2p member of the hsp70 family can form a stable, ATP-sensitive complex with HSF-a surprising finding because Ssb1/2p is not induced by heat shock. Phosphorylation and the assembly of HSF into larger, ATP-sensitive complexes both occur when HSF activity decreases, whether during adaptation to a raised temperature or during growth at low glucose concentrations. These larger HSF complexes also form during recovery from heat shock. However, if HSF is assembled into ATP-sensitive complexes (during growth at a low glucose concentration), heat shock does not stimulate the dissociation of the complexes. Nor does induction of the conformational change induce their dissociation. Modulation of the in vivo concentrations of the SSA and SSB proteins by deletion or overexpression affects HSF activity in a manner that is consistent with these findings and suggests the model that the SSA and SSB proteins perform distinct roles in the regulation of HSF activity. INTRODUCTIONIt has long been known that in cells of many species, including Escherichia coli and Saccharomyces cerevisiae, cell division rates are tightly coupled with the steady-state levels and rates of synthesis of ribosomal proteins and rRNA. For example, cells in rich media, with a short generation time, display higher abundance of rRNA and higher rates of synthesis of ribosomal proteins than do cells in poor media, with a long generation time. In E. coli, some of this regulation is achieved by transcriptional attenuation and translational regulation via binding of ribosomal proteins to the RNAs of target operons (Freedman et al., 1985;Cole and Nomura, 1986). In yeast, regulation is partly transcriptional, via RAP1 and its binding site, the upstream activating sequence (UAS) rpg (Herruer et al., 1987;Moehle and Hinnebusch, 1991;Kraakman et al., 1993), although much of the regulation of ribosomal protein abundance is achieved by a competition between the assembly into ribosomes and the rapid degradation of unassembled ribosomal proteins (Warner et al., 1985;Maicas et al., 1988).Growth rate control clearly modulates the level of the translational machinery, which in turn influences the overall rate of protein synthesis. Changes in the rates of protein synthesis must, in turn, have profound implications for the protein chaperone system. Newly synthesized polypeptides typically do not adopt their mature conformation immediately but instead follow a complex folding pathway. For many proteins, the cytoplasmic chaperone system plays an integral role in helping these polypeptides adopt their mature conformations (for review, see Hendrick and Hartl, 1995). The hsp70 proteins are generally believed to bind efficiently to nascent or newly synthesized polypeptides...

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Section: Discussionmentioning

confidence: 96%

Section: Discussionmentioning

confidence: 98%

Complex Regulation of the Yeast Heat Shock Transcription Factor

Bonner

Carlson

Fackenthal

et al. 2000

MBoC

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“…The metallothionein-encoding genes, CUP1 and CRS5, have also been shown to play a role in protecting yeast cells against oxidants (Culotta et al, 1994;Tamai et al, 1993). Moreover, expression of the CUP1 gene is inducible following exposure to the superoxide anion generator menadione and is important in conferring menadione resistance (Liu and Thiele, 1996).…”

Section: Introductionmentioning

confidence: 99%

The adaptive response of Saccharomyces cerevisiae to mercury exposure

Westwater

McLaren

Dormer

et al. 2002

Yeast

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The budding yeast Saccharomyces cerevisiae has been shown to possess a number of discrete but overlapping adaptive stress responses. We show here that yeast has an adaptive stress response towards mercury and that this response overlaps to some extent with the H 2 O 2 and cadmium-inducible stress responses. Expression of the yeast GSH1 gene, encoding c-glutamylcysteine synthetase, is known to be regulated by hydrogen peroxide; in this study we show that expression of a GSH1-lacZ reporter gene is shown to be regulated by exposure to heavy metals, such as mercury and cadmium. Other redoxactive metals, including copper and iron, were found not to induce GSH1 expression. We show that mercury-mediated regulation of the GSH1 gene is not by the same mechanism used by cadmium. Moreover, our experiments suggest the possibility that the oxidative stress produced by mercury exposure is similar to that produced by treatment with H 2 O 2 , consistent with our finding that the Yap1 protein is also involved in the response of yeast towards mercury.

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“…Several mutations in the DBD selectively affect transcription of the CUP1 gene, which contains a gap-type HSE (21)(22)(23)). The C-terminal activation domain termed AR2/CTA/CAD, but not the ScHsf1-specific N-terminal activation domain termed AR1/ NTA/AAD, is necessary for heat-and menadione-induced transcription of CUP1 (10,14,24). Deletion of AR2 also abrogates the heat shock response of several other genes containing gap-type HSEs (12).…”

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confidence: 99%

Interaction between Heat Shock Transcription Factors (HSFs) and Divergent Binding Sequences

Sakurai

Takemori

2007

Journal of Biological Chemistry

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The target genes of the heat shock transcription factor (HSF) contain a cis-acting sequence, the heat shock element (HSE), which consists of multiple inverted repeats of the sequence 5-nGAAn-3. Using data acquired in this and a previous study, we have identified the HSEs in 59 of 62 target genes of Saccharomyces cerevisiae Hsf1. The Hsf1 protein recognizes continuous and discontinuous repeats of the nGAAn unit; the nucleotide sequences and configuration of the units diverge slightly among functional HSEs. When Schizosaccharomyces pombe HSF was expressed in S. cerevisiae cells, heat shock induced S. pombe HSF to bind to various HSE types, which properly activated transcription from almost all target genes, suggesting that the S. pombe genome also contains divergent HSEs. Human HSF1 induced the heat shock response via HSEs with continuous units in S. cerevisiae cells but failed to do so via HSEs with discontinuous units. Binding of human HSF1 to the discontinuous type of HSE was observed in vitro but was significantly inhibited in vivo. These results show that human HSF1 recognizes HSEs in a slightly different way than yeast HSFs and suggest that the configuration of the unit is an important determinant for HSF-HSE interactions.

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Oxidative stress induced heat shock factor phosphorylation and HSF-dependent activation of yeast metallothionein gene transcription.

Cited by 150 publications

References 58 publications

Complex Regulation of the Yeast Heat Shock Transcription Factor

Complex Regulation of the Yeast Heat Shock Transcription Factor

The adaptive response of Saccharomyces cerevisiae to mercury exposure

Interaction between Heat Shock Transcription Factors (HSFs) and Divergent Binding Sequences

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