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Review

Biology of the Heat Shock Response and Protein Chaperones: Budding Yeast (Saccharomyces cerevisiae) as a Model System

Jacob Verghese, Jennifer Abrams, Yanyu Wang, Kevin A. Morano
Jacob Verghese
aDepartment of Microbiology and Molecular Genetics, University of Texas Medical School at Houston, Houston, Texas, USA
bGraduate School of Biomedical Sciences, University of Texas Health Science Center at Houston, Houston, Texas, USA
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Jennifer Abrams
aDepartment of Microbiology and Molecular Genetics, University of Texas Medical School at Houston, Houston, Texas, USA
bGraduate School of Biomedical Sciences, University of Texas Health Science Center at Houston, Houston, Texas, USA
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Yanyu Wang
aDepartment of Microbiology and Molecular Genetics, University of Texas Medical School at Houston, Houston, Texas, USA
bGraduate School of Biomedical Sciences, University of Texas Health Science Center at Houston, Houston, Texas, USA
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Kevin A. Morano
aDepartment of Microbiology and Molecular Genetics, University of Texas Medical School at Houston, Houston, Texas, USA
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DOI: 10.1128/MMBR.05018-11
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  • Fig 1
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    Fig 1

    Physiological effects of heat shock. Immediate consequences of thermal stress are depicted as described in the text. Relevant proteins are depicted as colored balls. Three response pathways are shown to be induced by heat shock: the CWI (cell wall integrity) pathway, the ESR (environmental stress response), and the HSR (heat shock response). The physiological effects of ceramide and long-chain base synthesis and accumulation after heat shock are unknown.

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    Fig 2

    Asymmetric distribution of damaged proteins during growth. Budding (predivision) and budded (postdivision) cells are depicted, with the net retention of damaged proteins in the mother cell resulting from Sir2-dependent transport. The two recently described “compartments” of protein aggregation, JUNQ and IPOD, are shown with known or suspected associated chaperones. Ub, ubiquitin; red asterisk, carbonylation or other protein damage; blue squiggle, unfolded protein.

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    Fig 3

    Hsf1 and Msn2/4, primary modulators of the heat shock response. Dashed lines represent postulated interactions of the Yak1 kinase in the regulation of both Msn2/4 and Hsf1. Red lines indicate regulatory interactions of protein kinase A. P, phosphorylation; STRE, stress response element; HSE, heat shock element.

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    Fig 4

    Architecture and regulation of yeast Hsf1. Relevant domains of the budding yeast transcription factor are indicated. Dashed lines represent regulatory relationships between the NTA (amino-terminal transactivation domain) and the CE2 (control element 2)/RD (regulatory domain) on the CTA (carboxy-terminal transactivation domain). The serine-rich region within the RD is phosphorylated by unknown kinases to promote the repression of the CTA through CE2. As described in the text, the NTA promotes a transient transcriptional response, whereas the CTA is responsible for sustained responses. DBD, DNA-binding domain; HRA/B/LZ, heptad repeats A and B, also called the leucine zipper; P, phosphorylation.

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    Fig 5

    The Hsp90 folding cycle. Yeast proteins participating in the Hsp90 folding cycle are indicated. The complexes depicted are from known yeast protein interactions or inferred from in vitro reconstitution experiments with metazoan counterparts, as described in the text. Unfolded client proteins are indicated by the wavy blue line, and the native folded state is labeled. Kinase clients are thought to mature through a Cdc37-specific pathway (kinases), while nearly all other clients proceed through the multichaperone pathway (nonkinases). The cyclophilin homolog Cpr7 (also Cpr6 [see the text]) is a TPR domain-containing protein that competes for binding with other TPR cofactors, including the phosphatase Ppt1, shown by the dashed line.

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    Fig 6

    The cytosolic disaggregation and refolding machinery. The native protein is shown to be unfolded by heat shock (depicted as a salmon rectangle), which also causes changes in the sHsp oligomerization status. The constitutive Ssa Hsp70 chaperones partner with the J protein Ydj1 and at least one nucleotide exchange factor (NEF) to promote the refolding of disaggregated (Hsp104 pathway) or unfolded but protected (Hsp42 and Hsp26) proteins.

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    Fig 7

    The ER chaperome. ER chaperones and associated cofactors are depicted, along with their respective roles in ER protein biogenesis. Gray 40S and 60S subunits depict docked ribosomes. S-S, disulfide bond; UPR, unfolded protein response.

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    Fig 8

    The mitochondrial chaperome. Chaperones and cofactors of the mitochondrion are shown. OM, outer membrane; IM, inner membrane; IMS, intermembrane space; TOM, transporter outer membrane complex; TIM, transporter inner membrane complex.

Tables

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  • Table 1

    Cytosolic chaperones

    ClassProtein(s)Function(s)
    Hsp100Hsp104Unfoldase; disaggregase
    Hsp90Hsp82Protein maturation, stress inducible
    Hsc82Protein maturation, constitutively expressed
        Hsp90 cochaperoneSti1Hsp70/Hsp90-organizing protein homolog, TPR containing
    Cns1Similar to Sti1, TPR containing
    Cdc37Protein kinase folding
    Sba1Hsp90 ATPase regulator
    Cpr6Immunophilin homolog, TPR containing, stress inducible
    Cpr7Immunophilin homolog, TPR containing, constitutively expressed
    Sgt1TPR-containing Hsp90 adaptor protein
    Aha1Hsp90 ATPase regulator
    Ppt1TPR-containing protein phosphatase
    Hsp70
        GRP170None
        Hsp110Sse1Hsp70 nucleotide exchange, substrate binding, constitutively expressed
    Sse2Hsp70 nucleotide exchange, substrate binding, stress inducible
        Hsp70Ssa1, Ssa2Protein folding, translocation, constitutively expressed
    Ssa3, Ssa4Protein folding, translocation, stress inducible
    Ssb1, Ssb2Nascent-chain folding
        Hsp70 NEFFes1Hsp70 nucleotide exchange
    Snl1Hsp70 nucleotide exchange, ER tethered
    Hsp40/J proteinYdj1Hsp70 ATPase activator, substrate binding
    Sis1Hsp70 ATPase activator, substrate binding
    Zuo1
    Caj1Hsp70 ATPase activator, substrate binding
    Djp1Hsp70 ATPase activator, substrate binding, peroxisomal import
    Xdj1Hsp70 ATPase activator, substrate binding
    Apj1Hsp70 ATPase activator, substrate binding
    Jjj1Hsp70 ATPase activator, ribosome biogenesis
    Jjj2Hsp70 ATPase activator
    Jjj3Hsp70 ATPase activator
    Hlj1Hsp70 ATPase activator, ERAD
    Cwc23Hsp70 ATPase activator, mRNA splicing
    Swa2Hsp70 ATPase activator, vesicle transport
    ChaperoninTriC/Cct1–Cct8Protein folding, cytoskeleton substrates
        Chaperonin cochaperonePfd1–Pfd6Protein folding, cytoskeleton substrates
    sHSPHsp42Antiaggregase
    Hsp26Antiaggregase
    OtherHsp12Membrane chaperone?
  • Table 2

    Endoplasmic reticulum chaperones

    ClassProteinFunction(s)
    Hsp100None
    Hsp90None
        Hsp90 cochaperoneNone
    Hsp70
        GRP170Lhs1Kar2 nucleotide exchange, substrate binding
        Hsp110None
        Hsp70Kar2Protein folding, translocation, UPR regulation, karyogamy
        Hsp70 NEFSil1Kar2 nucleotide exchange
    Hsp40/J proteinSec63Kar2 ATPase activator, translocation, ER membrane
    Scj1Kar2 ATPase activator
    Jem1Kar2 ATPase activator, karyogamy, ER membrane
    ChaperoninNone
        Chaperonin cochaperoneNone
    sHSPNone
    Other
        CalnexinCne1Folding of glycosylated proteins
        Protein disulfide isomerasePdi1Protein folding, disulfide redox chemistry
    Mpd1Protein folding, disulfide redox chemistry
    Mpd2Protein folding, disulfide redox chemistry
    Eug1Protein folding, disulfide redox chemistry?
    Eps1Protein folding, disulfide redox chemistry?, ER membrane
  • Table 3

    Mitochondrial chaperones

    ClassProteinFunction(s)
    Hsp100Hsp78Unfoldase, disaggregase
    Hsp90None
        Hsp90 cochaperoneNone
    Hsp70
        GRP170None
        Hsp110None
        Hsp70Ssc1Protein folding, translocation
    Ssc3Protein folding, translocation
    Ssq1Folding of FeS proteins
        Hsp70 NEFMge1Hsp70 nucleotide exchange
    Hsp40/J proteinMdj1Hsp70 ATPase stimulation, translocation
    Mdj2Hsp70 ATPase stimulation, translocation
    Jac1Ssq1 J-protein partner
    Pam16Partner with Pam18, Hsp70 ATPase stimulation, translocation
    Pam18Hsp70 ATPase stimulation, translocation
    ChaperoninHsp60Protein folding, translocation
        Chaperonin cochaperoneHsp10Partner with Hsp60, protein folding, translocation
    sHSPNone
    OtherHep1Ssc1 partner, stabilization
    Pim1Proteolysis and degradation
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Biology of the Heat Shock Response and Protein Chaperones: Budding Yeast (Saccharomyces cerevisiae) as a Model System
Jacob Verghese, Jennifer Abrams, Yanyu Wang, Kevin A. Morano
Microbiology and Molecular Biology Reviews Jun 2012, 76 (2) 115-158; DOI: 10.1128/MMBR.05018-11

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Biology of the Heat Shock Response and Protein Chaperones: Budding Yeast (Saccharomyces cerevisiae) as a Model System
Jacob Verghese, Jennifer Abrams, Yanyu Wang, Kevin A. Morano
Microbiology and Molecular Biology Reviews Jun 2012, 76 (2) 115-158; DOI: 10.1128/MMBR.05018-11
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  • Top
  • Article
    • SUMMARY
    • INTRODUCTION
    • PHYSIOLOGICAL EFFECTS OF HEAT SHOCK
    • TRANSCRIPTIONAL CONTROL OF THE HEAT SHOCK RESPONSE
    • MOLECULAR CHAPERONES OF THE CYTOPLASM
    • CHAPERONES OF THE SECRETORY PATHWAY
    • MOLECULAR CHAPERONES OF THE MITOCHONDRION
    • THE HSR IN PATHOGENIC FUNGI
    • ACKNOWLEDGMENTS
    • REFERENCES
    • Author Bios
  • Figures & Data
  • Info & Metrics
  • PDF

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