92155 Search Results


  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 86
    Santa Cruz Biotechnology 92155 hog1
    HSF1 overexpression induces filamentation independently of changes in <t>HSP90</t> transcript or protein levels, and function. a) To monitor the effects of HSF1 overexpression on filamentation independently of changes in HSP90 expression, we engineered strains where HSP90 is under the control of a constitutive promoter, ACT1p , in the tetO-HSF1/tetO-HSF1 strain. HSF1 and HSP90 transcript levels were normalized to ACT1 and GPD1 . Data are means +/- standard error of the means for triplicate samples. In the ACT1p-HSP90 strain, HSF1 levels are overexpressed (left panel) but HSP90 levels do not differ substantially from the wild-type levels (right panel). * indicates P value
    92155 Hog1, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/92155 hog1/product/Santa Cruz Biotechnology
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    92155 hog1 - by Bioz Stars, 2022-12
    86/100 stars
      Buy from Supplier

    Image Search Results


    HSF1 overexpression induces filamentation independently of changes in HSP90 transcript or protein levels, and function. a) To monitor the effects of HSF1 overexpression on filamentation independently of changes in HSP90 expression, we engineered strains where HSP90 is under the control of a constitutive promoter, ACT1p , in the tetO-HSF1/tetO-HSF1 strain. HSF1 and HSP90 transcript levels were normalized to ACT1 and GPD1 . Data are means +/- standard error of the means for triplicate samples. In the ACT1p-HSP90 strain, HSF1 levels are overexpressed (left panel) but HSP90 levels do not differ substantially from the wild-type levels (right panel). * indicates P value

    Journal: PLoS Genetics

    Article Title: Tuning Hsf1 levels drives distinct fungal morphogenetic programs with depletion impairing Hsp90 function and overexpression expanding the target space

    doi: 10.1371/journal.pgen.1007270

    Figure Lengend Snippet: HSF1 overexpression induces filamentation independently of changes in HSP90 transcript or protein levels, and function. a) To monitor the effects of HSF1 overexpression on filamentation independently of changes in HSP90 expression, we engineered strains where HSP90 is under the control of a constitutive promoter, ACT1p , in the tetO-HSF1/tetO-HSF1 strain. HSF1 and HSP90 transcript levels were normalized to ACT1 and GPD1 . Data are means +/- standard error of the means for triplicate samples. In the ACT1p-HSP90 strain, HSF1 levels are overexpressed (left panel) but HSP90 levels do not differ substantially from the wild-type levels (right panel). * indicates P value

    Article Snippet: Blots were hybridized with primary antibodies against the TAP epitope (1:3000, Thermo Fisher Scientific, CAB1001), pHog1 (1:1000, Phospho-p38 MAPK from Cell Signaling, 92155), Hog1 (1:1000–1:2500, Santa Cruz Biotechnology, SC 9079), Hsp90 (1:10,000, Bryan Larson), β-Actin (1:5000, Santa Cruz Biotechnology, SC 47778) or Tubulin (1:1000–1:5000, AbDseroTec, MCA78G) in block solution.

    Techniques: Over Expression, Expressing

    HSF1 depletion induces filamentation by compromising Hsp90 function, independently of changes in HSP90 expression. a) Western blot analysis was performed to assay if HSF1 depletion compromises Hsp90 function by monitoring the Hsp90 client protein Hog1. Strains were grown in the absence or presence of 20 μg/mL DOX. Cells were treated with 5 mM hydrogen peroxide (H 2 O 2 ) for 10 minutes to induce oxidative stress before protein extraction. Depletion of Hsf1 reduces the levels of phosphorylated Hog1 (pHog1) but not total Hog1 levels, even in the isogenic strain with constitutive HSP90 expression. Tubulin levels serve as loading control. WT indicates the wild type control. Experiment was performed in biological quadruplicate and a representative image is shown, with the western blots for the additional replicates shown in S8 Fig . b) HSF1 depletion causes a hypersensitivity to the Hsp90 inhibitor geldanamycin, even when HSP90 expression is constitutive and independent of Hsf1. Growth curves were generated by measuring the optical density of cells grown in the absence or presence of 20 μg/mL DOX in the presence of a concentration of geldanamycin that does not inhibit the growth of the wild-type strain (3.13 μM). Optical density at 595 nm was measured every 15 minutes with a TECAN plate reader grown with high orbital shaking at 30°C. Experiment was performed in biological quadruplicate, with one representative graph shown. c) HSF1 depletion causes filamentation at lower concentrations of geldanamycin (Gda) than is necessary to induce filamentation of the wild-type strain. Strains were grown in static conditions in the presence of no DOX or 20 μg/mL DOX, and in the presence of no geldanamycin (Gda) or 3.13 μM geldanamycin (Gda) at 30°C. In static growth conditions, 3.13 μM geldanamycin does not inhibit growth of the strains.

    Journal: PLoS Genetics

    Article Title: Tuning Hsf1 levels drives distinct fungal morphogenetic programs with depletion impairing Hsp90 function and overexpression expanding the target space

    doi: 10.1371/journal.pgen.1007270

    Figure Lengend Snippet: HSF1 depletion induces filamentation by compromising Hsp90 function, independently of changes in HSP90 expression. a) Western blot analysis was performed to assay if HSF1 depletion compromises Hsp90 function by monitoring the Hsp90 client protein Hog1. Strains were grown in the absence or presence of 20 μg/mL DOX. Cells were treated with 5 mM hydrogen peroxide (H 2 O 2 ) for 10 minutes to induce oxidative stress before protein extraction. Depletion of Hsf1 reduces the levels of phosphorylated Hog1 (pHog1) but not total Hog1 levels, even in the isogenic strain with constitutive HSP90 expression. Tubulin levels serve as loading control. WT indicates the wild type control. Experiment was performed in biological quadruplicate and a representative image is shown, with the western blots for the additional replicates shown in S8 Fig . b) HSF1 depletion causes a hypersensitivity to the Hsp90 inhibitor geldanamycin, even when HSP90 expression is constitutive and independent of Hsf1. Growth curves were generated by measuring the optical density of cells grown in the absence or presence of 20 μg/mL DOX in the presence of a concentration of geldanamycin that does not inhibit the growth of the wild-type strain (3.13 μM). Optical density at 595 nm was measured every 15 minutes with a TECAN plate reader grown with high orbital shaking at 30°C. Experiment was performed in biological quadruplicate, with one representative graph shown. c) HSF1 depletion causes filamentation at lower concentrations of geldanamycin (Gda) than is necessary to induce filamentation of the wild-type strain. Strains were grown in static conditions in the presence of no DOX or 20 μg/mL DOX, and in the presence of no geldanamycin (Gda) or 3.13 μM geldanamycin (Gda) at 30°C. In static growth conditions, 3.13 μM geldanamycin does not inhibit growth of the strains.

    Article Snippet: Blots were hybridized with primary antibodies against the TAP epitope (1:3000, Thermo Fisher Scientific, CAB1001), pHog1 (1:1000, Phospho-p38 MAPK from Cell Signaling, 92155), Hog1 (1:1000–1:2500, Santa Cruz Biotechnology, SC 9079), Hsp90 (1:10,000, Bryan Larson), β-Actin (1:5000, Santa Cruz Biotechnology, SC 47778) or Tubulin (1:1000–1:5000, AbDseroTec, MCA78G) in block solution.

    Techniques: Expressing, Western Blot, Protein Extraction, Generated, Concentration Assay

    Model for how HSF1 overexpression and depletion induce filamentation. Under basal conditions, HSF1 levels are moderate and C . albicans exists in the yeast form. A reduction in HSF1 levels leads to filamentous growth both by compromising Hsp90 function and through circuitry that is independent of Hsp90 but dependent on Efg1. An increase in HSF1 levels induces a dose-dependent expansion of Hsf1 direct targets that drives overexpression of positive regulators of morphogenesis, including Brg1 and Ume6, and decreased expression of negative regulators of morphogenesis, such as Nrg1, resulting in filamentous growth. Filaments induced by HSF1 overexpression and depletion are structurally distinct, require different genetic circuitry and are induced through distinct mechanisms.

    Journal: PLoS Genetics

    Article Title: Tuning Hsf1 levels drives distinct fungal morphogenetic programs with depletion impairing Hsp90 function and overexpression expanding the target space

    doi: 10.1371/journal.pgen.1007270

    Figure Lengend Snippet: Model for how HSF1 overexpression and depletion induce filamentation. Under basal conditions, HSF1 levels are moderate and C . albicans exists in the yeast form. A reduction in HSF1 levels leads to filamentous growth both by compromising Hsp90 function and through circuitry that is independent of Hsp90 but dependent on Efg1. An increase in HSF1 levels induces a dose-dependent expansion of Hsf1 direct targets that drives overexpression of positive regulators of morphogenesis, including Brg1 and Ume6, and decreased expression of negative regulators of morphogenesis, such as Nrg1, resulting in filamentous growth. Filaments induced by HSF1 overexpression and depletion are structurally distinct, require different genetic circuitry and are induced through distinct mechanisms.

    Article Snippet: Blots were hybridized with primary antibodies against the TAP epitope (1:3000, Thermo Fisher Scientific, CAB1001), pHog1 (1:1000, Phospho-p38 MAPK from Cell Signaling, 92155), Hog1 (1:1000–1:2500, Santa Cruz Biotechnology, SC 9079), Hsp90 (1:10,000, Bryan Larson), β-Actin (1:5000, Santa Cruz Biotechnology, SC 47778) or Tubulin (1:1000–1:5000, AbDseroTec, MCA78G) in block solution.

    Techniques: Over Expression, Expressing

    HSF1 depletion induces filamentation independently of changes in HSP90 expression. Strains were grown in the absence or presence of 20 μg/mL DOX in rich medium at 30°C. a) A strain was engineered where HSP90 is under the control of a constitutive promoter, ACT1p , in the tetO-HSF1/hsf1Δ background. In the ACT1p-HSP90 strain, HSF1 levels were depleted (left panel) with DOX without altering HSP90 expression (right panel). HSF1 and HSP90 transcript levels were normalized to ACT1 and GPD1 . Data are means +/- standard error of the means for triplicate samples. ** indicates P value

    Journal: PLoS Genetics

    Article Title: Tuning Hsf1 levels drives distinct fungal morphogenetic programs with depletion impairing Hsp90 function and overexpression expanding the target space

    doi: 10.1371/journal.pgen.1007270

    Figure Lengend Snippet: HSF1 depletion induces filamentation independently of changes in HSP90 expression. Strains were grown in the absence or presence of 20 μg/mL DOX in rich medium at 30°C. a) A strain was engineered where HSP90 is under the control of a constitutive promoter, ACT1p , in the tetO-HSF1/hsf1Δ background. In the ACT1p-HSP90 strain, HSF1 levels were depleted (left panel) with DOX without altering HSP90 expression (right panel). HSF1 and HSP90 transcript levels were normalized to ACT1 and GPD1 . Data are means +/- standard error of the means for triplicate samples. ** indicates P value

    Article Snippet: Blots were hybridized with primary antibodies against the TAP epitope (1:3000, Thermo Fisher Scientific, CAB1001), pHog1 (1:1000, Phospho-p38 MAPK from Cell Signaling, 92155), Hog1 (1:1000–1:2500, Santa Cruz Biotechnology, SC 9079), Hsp90 (1:10,000, Bryan Larson), β-Actin (1:5000, Santa Cruz Biotechnology, SC 47778) or Tubulin (1:1000–1:5000, AbDseroTec, MCA78G) in block solution.

    Techniques: Expressing

    The genetic circuitry through which Hsf1 and Hsp90 regulate filamentation are distinct. a) Filaments induced by compromised Hsp90 function are not dependent on the transcription factors Rob1 or Efg1, but are dependent on the protease Kex2 and the cell cycle checkpoint protein Bub2. Cultures were grown in the absence or presence of 10 μM of geldanamycin (Gda) for 6.5 hours to inhibit Hsp90 function. b) Unlike filaments induced by compromised Hsp90 function, filaments induced by HSF1 depletion are not dependent on Bub2 but are dependent on Efg1. Cultures were treated with no DOX, 0.1 μg/mL DOX (Low DOX), or 20 μg/mL DOX (High DOX) at 30°C. For both a) and b), blue outlines indicate that the homozygous deletion mutant of the morphogenetic regulator filaments to a comparable level as the non-mutant control and red outlines indicates that the mutant blocks filamentation.

    Journal: PLoS Genetics

    Article Title: Tuning Hsf1 levels drives distinct fungal morphogenetic programs with depletion impairing Hsp90 function and overexpression expanding the target space

    doi: 10.1371/journal.pgen.1007270

    Figure Lengend Snippet: The genetic circuitry through which Hsf1 and Hsp90 regulate filamentation are distinct. a) Filaments induced by compromised Hsp90 function are not dependent on the transcription factors Rob1 or Efg1, but are dependent on the protease Kex2 and the cell cycle checkpoint protein Bub2. Cultures were grown in the absence or presence of 10 μM of geldanamycin (Gda) for 6.5 hours to inhibit Hsp90 function. b) Unlike filaments induced by compromised Hsp90 function, filaments induced by HSF1 depletion are not dependent on Bub2 but are dependent on Efg1. Cultures were treated with no DOX, 0.1 μg/mL DOX (Low DOX), or 20 μg/mL DOX (High DOX) at 30°C. For both a) and b), blue outlines indicate that the homozygous deletion mutant of the morphogenetic regulator filaments to a comparable level as the non-mutant control and red outlines indicates that the mutant blocks filamentation.

    Article Snippet: Blots were hybridized with primary antibodies against the TAP epitope (1:3000, Thermo Fisher Scientific, CAB1001), pHog1 (1:1000, Phospho-p38 MAPK from Cell Signaling, 92155), Hog1 (1:1000–1:2500, Santa Cruz Biotechnology, SC 9079), Hsp90 (1:10,000, Bryan Larson), β-Actin (1:5000, Santa Cruz Biotechnology, SC 47778) or Tubulin (1:1000–1:5000, AbDseroTec, MCA78G) in block solution.

    Techniques: Mutagenesis