The Yeast Heat Shock Transcription Factor Changes Conformation in Response to Superoxide and Temperature

Lee, Sengyong; Carlson, Tage; Christian, Noah P.; Lea, Kristi; Kedzie, Jennifer; Reilly, James P.; Bonner, J. Jose

doi:10.1091/mbc.11.5.1753

Cited by 54 publications

(50 citation statements)

References 58 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We have shown that the conformational change can be induced by heat or superoxide acting directly on HSF (Lee et al, 2000), which suggests that a direct role of hsp70 may not be required for the activation of the heat shock response. We therefore seek a model for the role of the hsp70 proteins that accommodates both our biochemical data and the genetic data.…”

Section: Discussionmentioning

confidence: 94%

“…We have shown recently (Lee et al, 2000) that HSF undergoes a conformational change upon heat shock. This conformational change is detectable only in the context of two HSF trimers bound cooperatively to DNA.…”

Section: Hsf Complexes Do Not Dissociate Upon Superoxidestimulated Comentioning

confidence: 99%

“…It has been shown recently that HSF from both Drosophila and yeast is directly responsive to temperature (Zhong et al, 1998;Lee et al, 2000). It is thus possible that both HSF itself and hsp70 can serve as "cellular thermometers" in the activation of the heat shock response.…”

Section: Introductionmentioning

confidence: 99%

“…How can we integrate our findings with the current body of information about HSF and its regulation? The simplest view is that HSF is subject to several distinct modes of modification, each of which is somewhat independent of the others.With respect to the heat shock response per se, we adopt the concept that HSF responds to heat shock by conformational change, as suggested previously (Carr and Kim, 1993;Westwood and Wu, 1993;Zhong and Wu, 1996;Lee et al, 2000). We have shown that the conformational change can be induced by heat or superoxide acting directly on HSF (Lee et al, 2000), which suggests that a direct role of hsp70 may not be required for the activation of the heat shock response.…”

mentioning

confidence: 97%

See 3 more Smart Citations

Complex Regulation of the Yeast Heat Shock Transcription Factor

Bonner

Carlson

Fackenthal

et al. 2000

MBoC

Self Cite

View full text Add to dashboard Cite

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...

show abstract

Section: Discussionmentioning

confidence: 94%

Section: Hsf Complexes Do Not Dissociate Upon Superoxidestimulated Comentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 97%

See 2 more Smart Citations

Complex Regulation of the Yeast Heat Shock Transcription Factor

Bonner

Carlson

Fackenthal

et al. 2000

MBoC

Self Cite

View full text Add to dashboard Cite

show abstract

“…[126][127][128] Animal and yeast Hsfs have been found to act as direct ROS sensors. 129) Although yeast Hsf was found to be post-translationally activated by O À 2 , 130) human and Drosophila Hsfs directly sensed H 2 O 2 and assembled into a homotrimer as an active form in a reversible and redox-regulated manner. 131,132) Two Cys residues, located within and near the DNAbinding domain, were shown to be essential for the formation of intermolecular disulfide bonds, trimerization, and the nuclear localization of human Hsf in response to heat and H 2 O 2 .…”

Section: Common and Source-/kind-specific Ros Signaling Pathwaysmentioning

confidence: 99%

Cellular redox regulation, signaling, and stress response in plants

Shigeoka

Maruta

2014

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

Cellular and organellar redox states, which are characterized by the balance between oxidant and antioxidant pool sizes, play signaling roles in the regulation of gene expression and protein function in a wide variety of plant physiological processes including stress acclimation. Reactive oxygen species (ROS) and ascorbic acid (AsA) are the most abundant oxidants and antioxidants, respectively, in plant cells; therefore, the metabolism of these redox compounds must be strictly and spatiotemporally controlled. In this review, we provided an overview of our previous studies as well as recent advances in (1) the molecular mechanisms and regulation of AsA biosynthesis, (2) the molecular and genetic properties of ascorbate peroxidases, and (3) stress acclimation via ROS-derived oxidative/redox signaling pathways, and discussed future perspectives in this field.

show abstract

Current Awareness

2000

Yeast

View full text Add to dashboard Cite

In order to keep subscribers up‐to‐date with the latest developments in their field, this current awareness service is provided by John Wiley & Sons and contains newly‐published material on yeasts. Each bibliography is divided into 10 sections. 1 Books, Reviews & Symposia; 2 General; 3 Biochemistry; 4 Biotechnology; 5 Cell Biology; 6 Gene Expression; 7 Genetics; 8 Physiology; 9 Medical Mycology; 10 Recombinant DNA Technology. Within each section, articles are listed in alphabetical order with respect to author. If, in the preceding period, no publications are located relevant to any one of these headings, that section will be omitted. (3 weeks journals ‐ search completed 21st June 2000)

show abstract

The Yeast Heat Shock Transcription Factor Changes Conformation in Response to Superoxide and Temperature

Cited by 54 publications

References 58 publications

Complex Regulation of the Yeast Heat Shock Transcription Factor

Complex Regulation of the Yeast Heat Shock Transcription Factor

Cellular redox regulation, signaling, and stress response in plants

Current Awareness

Contact Info

Product

Resources

About