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https://www.readbyqxmd.com/read/27831465/dynamic-control-of-hsf1-during-heat-shock-by-a-chaperone-switch-and-phosphorylation
#1
Xu Zheng, Joanna Krakowiak, Nikit Patel, Ali Beyzavi, Jideofor Ezike, Ahmad S Khalil, David Pincus
Heat shock factor (Hsf1) regulates the expression of molecular chaperones to maintain protein homeostasis. Despite its central role in stress resistance, disease and aging, the mechanisms that control Hsf1 activity remain unresolved. Here we show that in budding yeast, Hsf1 basally associates with the chaperone Hsp70 and this association is transiently disrupted by heat shock, providing the first evidence that a chaperone repressor directly regulates Hsf1 activity. We develop and experimentally validate a mathematical model of Hsf1 activation by heat shock in which unfolded proteins compete with Hsf1 for binding to Hsp70...
November 10, 2016: ELife
https://www.readbyqxmd.com/read/27502399/size-doesn-t-matter-in-the-heat-shock-response
#2
David Pincus
Heat shock factor 1 (Hsf1) is a transcription factor that is often described as the master regulator of the heat shock response in all eukaryotes. However, due to its essentiality in yeast, Hsf1's contribution to the transcriptome under basal and heat shock conditions has never been directly determined. Using a chemical genetics approach that allowed rapid Hsf1 inactivation, my colleagues and I have recently shown that the bulk of the heat shock response is Hsf1 independent. Rather than inducing genes responsible for carrying out the various cellular processes required for adaptation to thermal stress, Hsf1 controls a dedicated set of chaperone protein genes devoted to restoring protein-folding homeostasis...
August 8, 2016: Current Genetics
https://www.readbyqxmd.com/read/27320198/defining-the-essential-function-of-yeast-hsf1-reveals-a-compact-transcriptional-program-for-maintaining-eukaryotic-proteostasis
#3
Eric J Solís, Jai P Pandey, Xu Zheng, Dexter X Jin, Piyush B Gupta, Edoardo M Airoldi, David Pincus, Vladimir Denic
Despite its eponymous association with the heat shock response, yeast heat shock factor 1 (Hsf1) is essential even at low temperatures. Here we show that engineered nuclear export of Hsf1 results in cytotoxicity associated with massive protein aggregation. Genome-wide analysis revealed that Hsf1 nuclear export immediately decreased basal transcription and mRNA expression of 18 genes, which predominately encode chaperones. Strikingly, rescuing basal expression of Hsp70 and Hsp90 chaperones enabled robust cell growth in the complete absence of Hsf1...
July 7, 2016: Molecular Cell
https://www.readbyqxmd.com/read/27185874/evidence-for-multiple-mediator-complexes-in-yeast-independently-recruited-by-activated-heat-shock-factor
#4
Jayamani Anandhakumar, Yara W Moustafa, Surabhi Chowdhary, Amoldeep S Kainth, David S Gross
Mediator is an evolutionarily conserved coactivator complex essential for RNA polymerase II transcription. Although it has been generally assumed that in Saccharomyces cerevisiae, Mediator is a stable trimodular complex, its structural state in vivo remains unclear. Using the "anchor away" (AA) technique to conditionally deplete select subunits within Mediator and its reversibly associated Cdk8 kinase module (CKM), we provide evidence that Mediator's tail module is highly dynamic and that a subcomplex consisting of Med2, Med3, and Med15 can be independently recruited to the regulatory regions of heat shock factor 1 (Hsf1)-activated genes...
July 15, 2016: Molecular and Cellular Biology
https://www.readbyqxmd.com/read/27050263/purification-crystallization-and-x-ray-diffraction-analysis-of-the-dna-binding-domain-of-human-heat-shock-factor-2
#5
Han Feng, Wei Liu, Da Cheng Wang
Cells respond to various proteotoxic stimuli and maintain protein homeostasis through a conserved mechanism called the heat-shock response, which is characterized by the enhanced synthesis of heat-shock proteins. This response is mediated by heat-shock factors (HSFs). Four genes encoding HSF1-HSF4 exist in the genome of mammals. In this protein family, HSF1 is the orthologue of the single HSF in lower eukaryotic organisms and is the major regulator of the heat-shock response, while HSF2, which shows low sequence homology to HSF1, serves as a developmental regulator...
April 2016: Acta Crystallographica. Section F, Structural Biology Communications
https://www.readbyqxmd.com/read/27033550/spatial-sequestration-and-detoxification-of-huntingtin-by-the-ribosome-quality-control-complex
#6
Junsheng Yang, Xinxin Hao, Xiuling Cao, Beidong Liu, Thomas Nyström
Huntington disease (HD) is a neurological disorder caused by polyglutamine expansions in mutated Huntingtin (mHtt) proteins, rendering them prone to form inclusion bodies (IB). We report that in yeast, such IB formation is a factor-dependent process subjected to age-related decline. A genome-wide, high-content imaging approach, identified the E3 ubiquitin ligase, Ltn1 of the ribosome quality control complex (RQC) as a key factor required for IB formation, ubiquitination, and detoxification of model mHtt. The failure of ltn1∆ cells to manage mHtt was traced to another RQC component, Tae2, and inappropriate control of heat shock transcription factor, Hsf1, activity...
2016: ELife
https://www.readbyqxmd.com/read/27017930/huntingtin-interacting-protein-hypk-is-a-negative-regulator-of-heat-shock-response-and-is-downregulated-in-models-of-huntington-s-disease
#7
Srijit Das, Nitai Pada Bhattacharyya
Huntingtin interacting protein HYPK (Huntingtin Yeast Partner K) is an intrinsically unstructured protein having chaperone-like activity and can suppress mutant huntingtin aggregates and toxicity in cell model of Huntington's Disease (HD). Heat shock response is an adaptive mechanism of cells characterized by upregulation of heat shock proteins by heat-induced activation of heat shock factor 1 (HSF1). The trans-activation ability of HSF1 is arrested upon restoration of proteostasis. We earlier identified HYPK as a heat-inducible protein and transcriptional target of HSF1...
May 1, 2016: Experimental Cell Research
https://www.readbyqxmd.com/read/25934390/yeast-tolerance-to-various-stresses-relies-on-the-trehalose-6p-synthase-tps1-protein-not-on-trehalose
#8
Marjorie Petitjean, Marie-Ange Teste, Jean M François, Jean-Luc Parrou
Trehalose is a stable disaccharide commonly found in nature, from bacteria to fungi and plants. For the model yeast Saccharomyces cerevisiae, claims that trehalose is a stress protectant were based indirectly either on correlation between accumulation of trehalose and high resistance to various stresses or on stress hypersensitivity of mutants deleted for TPS1, which encodes the first enzyme in trehalose biosynthetic pathway. Our goal was to investigate more directly which one, between trehalose and/or the Tps1 protein, may serve yeast cells to withstand exposure to stress...
June 26, 2015: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/25511255/iron-copper-and-manganese-complexes-with-in-vitro-superoxide-dismutase-and-or-catalase-activities-that-keep-saccharomyces-cerevisiae-cells-alive-under-severe-oxidative-stress
#9
Thales P Ribeiro, Christiane Fernandes, Karen V Melo, Sarah S Ferreira, Josane A Lessa, Roberto W A Franco, Gerhard Schenk, Marcos D Pereira, Adolfo Horn
Due to their aerobic lifestyle, eukaryotic organisms have evolved different strategies to overcome oxidative stress. The recruitment of some specific metalloenzymes such as superoxide dismutases (SODs) and catalases (CATs) is of great importance for eliminating harmful reactive oxygen species (hydrogen peroxide and superoxide anion). Using the ligand HPClNOL {1-[bis(pyridin-2-ylmethyl)amino]-3-chloropropan-2-ol}, we have synthesized three coordination compounds containing iron(III), copper(II), and manganese(II) ions, which are also present in the active site of the above-noted metalloenzymes...
March 2015: Free Radical Biology & Medicine
https://www.readbyqxmd.com/read/25119046/promoter-sequences-direct-cytoplasmic-localization-and-translation-of-mrnas-during-starvation-in-yeast
#10
Brian M Zid, Erin K O'Shea
A universal feature of the response to stress and nutrient limitation is transcriptional upregulation of genes that encode proteins important for survival. Under many such conditions, the overall protein synthesis level is reduced, thereby dampening the stress response at the level of protein expression. For example, during glucose starvation in Saccharomyces cerevisiae (yeast), translation is rapidly repressed, yet the transcription of many stress- and glucose-repressed genes is increased. Here we show, using ribosomal profiling and microscopy, that this transcriptionally upregulated gene set consists of two classes: one class produces messenger RNAs that are translated during glucose starvation and are diffusely localized in the cytoplasm, including many heat-shock protein mRNAs; and the other class produces mRNAs that are not efficiently translated during glucose starvation and are concentrated in foci that co-localize with P bodies and stress granules, a class that is enriched for mRNAs involved in glucose metabolism...
October 2, 2014: Nature
https://www.readbyqxmd.com/read/25078989/immunolocalization-of-anti-hsf1-to-the-acetabular-glands-of-infectious-schistosomes-suggests-a-non-transcriptional-function-for-this-transcriptional-activator
#11
Kenji Ishida, Melissa Varrecchia, Giselle M Knudsen, Emmitt R Jolly
Schistosomiasis is a chronically debilitating disease caused by parasitic worms of the genus Schistosoma, and it is a global problem affecting over 240 million people. Little is known about the regulatory proteins and mechanisms that control schistosome host invasion, gene expression, and development. Schistosome larvae, cercariae, are transiently free-swimming organisms and infectious to man. Cercariae penetrate human host skin directly using proteases that degrade skin connective tissue. These proteases are secreted from anucleate acetabular glands that contain many proteins, including heat shock proteins...
2014: PLoS Neglected Tropical Diseases
https://www.readbyqxmd.com/read/24970820/insights-from-yeast-into-whether-the-inhibition-of-heat-shock-transcription-factor-hsf1-by-rapamycin-can-prevent-the-hsf1-activation-that-results-from-treatment-with-an-hsp90-inhibitor
#12
Stefan H Millson, Peter W Piper
UNLABELLED: In human cells TORC1 mTOR (target of rapamycin) protein kinase complex renders heat shock transcription factor 1 (Hsf1) competent for stress activation. In such cells, as well as in yeast, the selective TORC1 inhibitor rapamycin blocks this activation in contrast to Hsp90 inhibitors which potently activate Hsf1. Potentially therefore rapamycin could prevent the Hsf1 activation that frequently compromises the efficiency of Hsp90 inhibitor cancer drugs. Little synergy was found between the effects of rapamycin and the Hsp90 inhibitor radicicol on yeast growth...
July 15, 2014: Oncotarget
https://www.readbyqxmd.com/read/24951438/membrane-fluidity-and-temperature-sensing-are-coupled-via-circuitry-comprised-of-ole1-rsp5-and-hsf1-in-candida-albicans
#13
Michelle D Leach, Leah E Cowen
Temperature is a ubiquitous environmental variable which can profoundly influence the physiology of living cells as it changes over time and space. When yeast cells are exposed to a sublethal heat shock, normal metabolic functions become repressed and the heat shock transcription factor Hsf1 is activated, inducing heat shock proteins (HSPs). Candida albicans, the most prevalent human fungal pathogen, is an opportunistic pathogen that has evolved as a relatively harmless commensal of healthy individuals. Even though C...
August 2014: Eukaryotic Cell
https://www.readbyqxmd.com/read/24800749/inhibiting-heat-shock-factor-1-in-human-cancer-cells-with-a-potent-rna-aptamer
#14
H Hans Salamanca, Marc A Antonyak, Richard A Cerione, Hua Shi, John T Lis
Heat shock factor 1 (HSF1) is a master regulator that coordinates chaperone protein expression to enhance cellular survival in the face of heat stress. In cancer cells, HSF1 drives a transcriptional program distinct from heat shock to promote metastasis and cell survival. Its strong association with the malignant phenotype implies that HSF1 antagonists may have general and effective utilities in cancer therapy. For this purpose, we had identified an avid RNA aptamer for HSF1 that is portable among different model organisms...
2014: PloS One
https://www.readbyqxmd.com/read/24671421/hierarchical-functional-specificity-of-cytosolic-heat-shock-protein-70-hsp70-nucleotide-exchange-factors-in-yeast
#15
Jennifer L Abrams, Jacob Verghese, Patrick A Gibney, Kevin A Morano
Heat shock protein 70 (Hsp70) molecular chaperones play critical roles in protein homeostasis. In the budding yeast Saccharomyces cerevisiae, cytosolic Hsp70 interacts with up to three types of nucleotide exchange factors (NEFs) homologous to human counterparts: Sse1/Sse2 (Heat shock protein 110 (Hsp110)), Fes1 (HspBP1), and Snl1 (Bag-1). All three NEFs stimulate ADP release; however, it is unclear why multiple distinct families have been maintained throughout eukaryotic evolution. In this study we investigate NEF roles in Hsp70 cell biology using an isogenic combinatorial collection of NEF deletion mutants...
May 9, 2014: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/24465598/transcription-regulation-of-hypk-by-heat-shock-factor-1
#16
Srijit Das, Nitai Pada Bhattacharyya
HYPK (Huntingtin Yeast Partner K) was originally identified by yeast two-hybrid assay as an interactor of Huntingtin, the protein mutated in Huntington's disease. HYPK was characterized earlier as an intrinsically unstructured protein having chaperone-like activity in vitro and in vivo. HYPK has the ability of reducing rate of aggregate formation and subsequent toxicity caused by mutant Huntingtin. Further investigation revealed that HYPK is involved in diverse cellular processes and required for normal functioning of cells...
2014: PloS One
https://www.readbyqxmd.com/read/24146635/hsp70-hsp40-chaperone-complex-functions-in-controlling-polarized-growth-by-repressing-hsf1-driven-heat-stress-associated-transcription
#17
Aleksandar Vjestica, Dan Zhang, Jianhua Liu, Snezhana Oliferenko
How the molecular mechanisms of stress response are integrated at the cellular level remains obscure. Here we show that the cellular polarity machinery in the fission yeast Schizosaccharomyces pombe undergoes dynamic adaptation to thermal stress resulting in a period of decreased Cdc42 activity and altered, monopolar growth. Cells where the heat stress-associated transcription was genetically upregulated exhibit similar growth patterning in the absence of temperature insults. We identify the Ssa2-Mas5/Hsp70-Hsp40 chaperone complex as repressor of the heat shock transcription factor Hsf1...
2013: PLoS Genetics
https://www.readbyqxmd.com/read/24126084/characterization-of-global-gene-expression-during-assurance-of-lifespan-extension-by-caloric-restriction-in-budding-yeast
#18
Kyung-Mi Choi, Young-Yon Kwon, Cheol-Koo Lee
Caloric restriction (CR) is the best-studied intervention known to delay aging and extend lifespan in evolutionarily distant organisms ranging from yeast to mammals in the laboratory. Although the effect of CR on lifespan extension has been investigated for nearly 80years, the molecular mechanisms of CR are still elusive. Consequently, it is important to understand the fundamental mechanisms of when and how lifespan is affected by CR. In this study, we first identified the time-windows during which CR assured cellular longevity by switching cells from culture media containing 2% or 0...
December 2013: Experimental Gerontology
https://www.readbyqxmd.com/read/23733891/genetic-selection-for-constitutively-trimerized-human-hsf1-mutants-identifies-a-role-for-coiled-coil-motifs-in-dna-binding
#19
Daniel W Neef, Alex M Jaeger, Dennis J Thiele
Human heat shock transcription factor 1 (HSF1) promotes the expression of stress-responsive genes and is a critical factor for the cellular protective response to proteotoxic and other stresses. In response to stress, HSF1 undergoes a transition from a repressed cytoplasmic monomer to a homotrimer, accumulates in the nucleus, binds DNA, and activates target gene transcription. Although these steps occur as sequential and highly regulated events, our understanding of the full details of the HSF1 activation pathway remains incomplete...
August 2013: G3: Genes—Genomes—Genetics
https://www.readbyqxmd.com/read/23447536/mediator-recruitment-to-heat-shock-genes-requires-dual-hsf1-activation-domains-and-mediator-tail-subunits-med15-and-med16
#20
Sunyoung Kim, David S Gross
The evolutionarily conserved Mediator complex is central to the regulation of gene transcription in eukaryotes because it serves as a physical and functional interface between upstream regulators and the Pol II transcriptional machinery. Nonetheless, its role appears to be context-dependent, and the detailed mechanism by which it governs the expression of most genes remains unknown. Here we investigate Mediator involvement in HSP (heat shock protein) gene regulation in the yeast Saccharomyces cerevisiae. We find that in response to thermal upshift, subunits representative of each of the four Mediator modules (Head, Middle, Tail, and Kinase) are rapidly, robustly, and selectively recruited to the promoter regions of HSP genes...
April 26, 2013: Journal of Biological Chemistry
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