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A stress regulatory network for co-ordinated activation of proteasome expression mediated by yeast heat shock transcription factor.
Mol Microbiol. 2006 Apr; 60(1):240-51.MM

Abstract

Heat shock transcription factor (HSF) mediates the transcriptional response of eukaryotic cells to heat, infection and inflammation, pharmacological agents, and other stresses. Although genes encoding heat shock proteins (HSPs) are the best characterized targets of HSF, recent genome-wide localization of Saccharomyces cerevisiae HSF revealed novel HSF targets involved in a wide range of cellular functions. One such target, the RPN4 gene, encodes a transcription factor that directly activates expression of a number of genes encoding proteasome subunits. Here we demonstrate that HSF co-ordinates a feed-forward gene regulatory circuit for RPN4 activation. We show that HSF activates expression of PDR3, encoding a multidrug resistance (MDR) transcription factor that also directly activates RPN4 gene expression. We demonstrate that the HSF binding site (HSE) in the RPN4 promoter is primarily responsible for heat- or methyl methanesulphonate induction of RPN4, with a minor contribution of Pdr3 binding sites (PDREs), while a Yap1 binding site (YRE) is responsible for RPN4 induction in response to oxidative stress. Furthermore, heat-induced expression of Rpn4 protein leads to expression of Rpn4 targets at later stages of heat stress, providing a temporal controlling mechanism for proteasome synthesis upon stress conditions that could result in irreversibly damaged proteins. In addition, the overlapping transcriptional regulatory networks involving HSF, Yap1 and Pdr3 suggest a close linkage between stress responses and pleiotropic drug resistance.

Authors+Show Affiliations

Hahn JS
School of Chemical and Biological Engineering, Seoul National University, Seoul 151-744, Korea.
Neef DW
No affiliation info available
Thiele DJ
No affiliation info available

MeSH

Binding SitesDNA-Binding ProteinsDrug Resistance, MicrobialGene Expression Regulation, FungalHeat-Shock ProteinsHeat-Shock ResponseMethyl MethanesulfonatePromoter Regions, GeneticProteasome Endopeptidase ComplexSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription Factors

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural

Language

eng

PubMed ID

16556235

Citation

Hahn, Ji-Sook, et al. "A Stress Regulatory Network for Co-ordinated Activation of Proteasome Expression Mediated By Yeast Heat Shock Transcription Factor." Molecular Microbiology, vol. 60, no. 1, 2006, pp. 240-51.
Hahn JS, Neef DW, Thiele DJ. A stress regulatory network for co-ordinated activation of proteasome expression mediated by yeast heat shock transcription factor. Mol Microbiol. 2006;60(1):240-51.
Hahn, J. S., Neef, D. W., & Thiele, D. J. (2006). A stress regulatory network for co-ordinated activation of proteasome expression mediated by yeast heat shock transcription factor. Molecular Microbiology, 60(1), 240-51.
Hahn JS, Neef DW, Thiele DJ. A Stress Regulatory Network for Co-ordinated Activation of Proteasome Expression Mediated By Yeast Heat Shock Transcription Factor. Mol Microbiol. 2006;60(1):240-51. PubMed PMID: 16556235.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A stress regulatory network for co-ordinated activation of proteasome expression mediated by yeast heat shock transcription factor. AU - Hahn,Ji-Sook, AU - Neef,Daniel W, AU - Thiele,Dennis J, PY - 2006/3/25/pubmed PY - 2006/6/28/medline PY - 2006/3/25/entrez SP - 240 EP - 51 JF - Molecular microbiology JO - Mol Microbiol VL - 60 IS - 1 N2 - Heat shock transcription factor (HSF) mediates the transcriptional response of eukaryotic cells to heat, infection and inflammation, pharmacological agents, and other stresses. Although genes encoding heat shock proteins (HSPs) are the best characterized targets of HSF, recent genome-wide localization of Saccharomyces cerevisiae HSF revealed novel HSF targets involved in a wide range of cellular functions. One such target, the RPN4 gene, encodes a transcription factor that directly activates expression of a number of genes encoding proteasome subunits. Here we demonstrate that HSF co-ordinates a feed-forward gene regulatory circuit for RPN4 activation. We show that HSF activates expression of PDR3, encoding a multidrug resistance (MDR) transcription factor that also directly activates RPN4 gene expression. We demonstrate that the HSF binding site (HSE) in the RPN4 promoter is primarily responsible for heat- or methyl methanesulphonate induction of RPN4, with a minor contribution of Pdr3 binding sites (PDREs), while a Yap1 binding site (YRE) is responsible for RPN4 induction in response to oxidative stress. Furthermore, heat-induced expression of Rpn4 protein leads to expression of Rpn4 targets at later stages of heat stress, providing a temporal controlling mechanism for proteasome synthesis upon stress conditions that could result in irreversibly damaged proteins. In addition, the overlapping transcriptional regulatory networks involving HSF, Yap1 and Pdr3 suggest a close linkage between stress responses and pleiotropic drug resistance. SN - 0950-382X UR - https://www.unboundmedicine.com/medline/citation/16556235/A_stress_regulatory_network_for_co_ordinated_activation_of_proteasome_expression_mediated_by_yeast_heat_shock_transcription_factor_ DB - PRIME DP - Unbound Medicine ER -