The GCN4 leucine zipper can functionally substitute for the heat shock transcription factor’s trimerization domain

Drees, Becky; Grotkopp, E.; Nelson, Hillary C. M.

doi:10.1006/jmbi.1997.1283

Cited by 30 publications

(30 citation statements)

References 70 publications

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“…Although a sequence containing two tandem nTTCn units binds eukaryotic HSFs (8,43,44), the presence of the third unit with the 5-bp spacing is essential for efficient recognition and for heat-induced transcription by Hsf1. Two DBDs may bind asymmetrically to the two neighboring tandem nTTCn units (8,(43)(44)(45), although it remains to be resolved how the trimeric Hsf1 binds simultaneously to the three nTTCn units. Interactions with direct or inverted recognition sequences are well characterized in transcription factors that form dimers.…”

Section: Discussionmentioning

confidence: 99%

“…The formation of the DNA⅐Hsf1 complex was inhibited by addition of increasing amounts of unlabeled SSC1wt fragment (lanes 3 and 4) but was not significantly affected by fragments containing the mutated sequences (lanes 5-14). In vitro, Saccharomyces Hsf1 and Drosophila HSF are able to bind to a sequence consisting of two nTTCn tandem units with the 5-bp spacing but with a binding affinity significantly lower relative to the perfect-type HSE (8,43,44). In vivo, various derivatives of two tandem units were not able to mediate a heat shock response (Fig.…”

Section: Genome-wide Transcriptional Changes In Cells Bearing the Hsfmentioning

confidence: 98%

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Identification of a Novel Class of Target Genes and a Novel Type of Binding Sequence of Heat Shock Transcription Factor in Saccharomyces cerevisiae

Yamamoto

Mizukami

Sakurai

2005

Journal of Biological Chemistry

159

177

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In response to hyperthermia, heat shock transcription factor (HSF) activates transcription of a set of genes encoding heat shock proteins (HSPs). The promoter regions of HSP genes contain the HSF binding sequence called the heat shock element (HSE), which consists of contiguous inverted repeats of the sequence 5-nGAAn-3 (where n is any nucleotide). We have constructed an hsf1 mutant of Saccharomyces cerevisiae and analyzed genome-wide changes in heat shock response in the mutant cells. The results have revealed that Hsf1 is necessary for heat-induced transcription of not only HSP but also genes encoding proteins involved in diverse cellular processes such as protein degradation, detoxification, energy generation, carbohydrate metabolism, and maintenance of cell wall integrity. Approximately half of the Hsf1-regulated genes lacked the typical HSE in their promoter regions. Instead, several of these genes have a novel Hsf1 binding sequence that contains three direct repeats of nTTCn (or nGAAn) interrupted by 5 bp. The number and spacing of the repeating units are critical determinants for heat-induced transcription as well as for recognition by Hsf1. In the yeast genome, the presence of the sequence is enriched in Hsf1-regulated genes, suggesting that it is generally used as an HSE in the Hsf1 regulon.

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Section: Discussionmentioning

confidence: 99%

Section: Genome-wide Transcriptional Changes In Cells Bearing the Hsfmentioning

confidence: 98%

Identification of a Novel Class of Target Genes and a Novel Type of Binding Sequence of Heat Shock Transcription Factor in Saccharomyces cerevisiae

Yamamoto

Mizukami

Sakurai

2005

Journal of Biological Chemistry

159

177

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“…Secondary structure characteristics, included below the sequence, are based on the K. lactis structure (12). protocols (13,31). Plasmid pBL3 (31), which contains an HSE with three GAA repeats, was digested with XhoI and SpeI.…”

Section: Methodsmentioning

confidence: 99%

“…protocols (13,31). Plasmid pBL3 (31), which contains an HSE with three GAA repeats, was digested with XhoI and SpeI. The 145-base pair fragment was purified on a 4% Metaphor (BMA)-agarose gel and the ends were labeled with T4 polynucleotide kinase and [␥-32 P]ATP.…”

Section: Methodsmentioning

confidence: 99%

“…␥-32 P-Labeled 145-base pair fragment (0.75 fmol) was mixed with a protein sample (1.8 fmol to 20 pmol) in a final volume of 20 l and incubated at room temperature for 10 min. Reactions were loaded onto polyacrylamide gels and electrophoresed as described previously (31). Dried gels were used to expose Molecular Dynamics PhosphorImager plates, and data were analyzed as described previously (13).…”

Section: Methodsmentioning

confidence: 99%

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The DNA-binding Domain of Yeast Heat Shock Transcription Factor Independently Regulates Both the N- and C-terminal Activation Domains

Bulman¹,

Hubl²,

Nelson³

2001

Journal of Biological Chemistry

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The expression of heat shock proteins in response to cellular stresses is dependent on the activity of the heat shock transcription factor (HSF). In yeast, HSF is constitutively bound to DNA; however, the mitigation of negative regulation in response to stress dramatically increases transcriptional activity. Through alaninescanning mutagenesis of the surface residues of the DNA-binding domain, we have identified a large number of mutants with increased transcriptional activity. Six of the strongest mutations were selected for detailed study. Our studies suggest that the DNA-binding domain is involved in the negative regulation of both the Nterminal and C-terminal activation domains of HSF. These mutations do not significantly affect DNA binding. Circular dichroism analysis suggests that a subset of the mutants may have altered secondary structure, whereas a different subset has decreased thermal stability. Our findings suggest that the regulation of HSF transcriptional activity (under both constitutive and stressed conditions) may be partially dependent on the local topology of the DNA-binding domain. In addition, the DNA-binding domain may mediate key interactions with ancillary factors and/or other intramolecular regulatory regions in order to modulate the complex regulation of HSF's transcriptional activity.

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Role of an α-helical bulge in the yeast heat shock transcription factor 1 1Edited by F. E. Cohen

Hardy

Walsh

Nelson

2000

Journal of Molecular Biology

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The GCN4 leucine zipper can functionally substitute for the heat shock transcription factor’s trimerization domain

Cited by 30 publications

References 70 publications

Identification of a Novel Class of Target Genes and a Novel Type of Binding Sequence of Heat Shock Transcription Factor in Saccharomyces cerevisiae

Identification of a Novel Class of Target Genes and a Novel Type of Binding Sequence of Heat Shock Transcription Factor in Saccharomyces cerevisiae

The DNA-binding Domain of Yeast Heat Shock Transcription Factor Independently Regulates Both the N- and C-terminal Activation Domains

Role of an α-helical bulge in the yeast heat shock transcription factor 1 1Edited by F. E. Cohen

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