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  • 1
    Electronic Resource
    Electronic Resource
    Upregulation of the Hsp104 chaperone at physiological temperature during recovery from thermal insult (2004)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 52 (2004), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Thermal insult at 50°C causes protein denaturation in yeast, but the cells survive if preconditioned at 37°C. Survival depends on refolding of heat-denatured proteins. Refolding of cytoplasmic proteins requires Hsp104, the expression of which increases several-fold upon shift of the cells from physiological temperature 24°C to 37°C. We describe here a novel type of regulation of Hsp104, designated delayed upregulation (DUR). When Saccharomyces cerevisiae cells grown at 24°C, preconditioned at 37°C and treated briefly at 50°C were shifted back to 24°C, Hsp104 expression was negligible for 1 h, but increased then to a three to nine times higher level than that detected after growth at 24°C, returning to normal after 5 h. A heat shock element (HSE) of the upstream sequence of HSP104 was necessary and sufficient for DUR, whereas stress response elements (STRE) were dispensable. Destruction of HSE plus all three STREs abolished Hsp104 expression, resulting in cell death after thermal insult. Deletion of MSN2/4, encoding transcription factors driving STRE-dependent gene expression, decreased DUR. Deletion of HOG1, encoding a heat-responsive and osmosensitive mitogen-activated protein kinase implicated to be functionally connected to Msn2/4p, abolished DUR. We suggest that DUR was regulated via HSE, required Hog1p and involved Msn2/4p-regulated gene products.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.2003.03959.x
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  • 2
    Electronic Resource
    Electronic Resource
    Trehalose is required for conformational repair of heat-denatured proteins in the yeast endoplasmic reticulum but not for maintenance of membrane traffic functions after severe heat stress (2000)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 37 (2000), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Saccharomyces cerevisiae cells grown at physiological temperature 24°C require preconditioning at 37°C to acquire tolerance towards brief exposure to 48–50°C. During preconditioning, the cytosolic trehalose content increases remarkably and in the absence of trehalose synthesis yeast cannot acquire thermotolerance. It has been speculated that trehalose protects proteins and membranes under environmental stress conditions, but recently it was shown to assist the Hsp104 chaperone in refolding of heat-damaged proteins in the yeast cytosol. We have demonstrated that heat-denatured proteins residing in the endoplasmic reticulum (ER) also can be refolded once the cells are returned to physiological temperature. Unexpectedly, not only ER chaperones but also the cytosolic Hsp104 chaperone is required for conformational repair events in the ER lumen. Here we show that trehalose facilitates refolding of glycoproteins in the ER after severe heat stress. In the absence of Tps1p, a subunit of trehalose synthase, refolding of heat-damaged glycoproteins to bioactive and secretion-competent forms failed or was retarded. In contrast, membrane traffic operated many hours after severe heat stress even in the absence of the TPS1 gene, demonstrating that trehalose had no role in thermoprotection of membranes engaged in vesicular traffic. However, cytosolic proteins were aggregated and protein synthesis abolished, resulting finally in cell death.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.2000.01970.x
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  • 3
    Electronic Resource
    Electronic Resource
    Low Molecular Weight High–Mannose Type Glycans in a Secreted Protein of the Filamentous Fungus Trichoderma Reesei (1987)
    [s.l.] : Nature Publishing Company
    Nature biotechnology 5 (1987), S. 152-156 
    Details
    ISSN: 1546-1696
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: [Auszug] With the object of obtaining information about the suitability of filamentous fungi for production of heterogeneous mammalian proteins, we have characterized the normal glycosylation pattern of CBH I, the major glycoprotein secreted by Trichoderma reesei. The protein–bound glycans of CBH I ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nbt0287-152
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  • 4
    Electronic Resource
    Electronic Resource
    Dual regulation by heat and nutrient stress of the yeast HSP150 gene encoding a secretory glycoprotein (1993)
    Springer
    Molecular genetics and genomics 239 (1993), S. 273-280 
    Details
    ISSN: 1617-4623
    Keywords: Heat shock gene ; Heat shock protein ; Secretion ; Yeast ; Transcription
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have cloned and characterized the HSP150 gene of Saccharomyces cerevisiae, which encodes a glycoprotein (hsp150) that is secreted into the growth medium. Unexpectedly, the HSP150 gene was found to be regulated by heat shock and nitrogen starvation. Shifting the cells from 24° C to 37° C resulted in an abrupt increase in the steady-state level of the HSP150 mRNA, and de novo synthesized hsp150 protein. Returning the cells to 24° C caused a rapid decrease in mRNA and protein synthesis to basal levels. The HSP150 5′-flanking region contains several heat shock element-like sequences (HSE). To study the function of these sequences, a strain bearing a disrupted copy of the HSP150 gene was transformed with plasmids in which the coding region of HSP150, or a HSP150-lacZ fusion gene, was preceded by 5′ deletion derivatives of the HSP150 promoter. Site-directed mutagenesis of one HSE-like element, located between the TATA box and transcription initiation sites, abolished heat activation of transcription. In addition to heat shock, the HSP150 gene is regulated by the availability of nutrients in the growth medium. The HSP150 mRNA level was increased by nitrogen limitation at 24° C, even when under the control of a HSP150 promoter region of 137 by carrying the mutagenized HSE.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00281628
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  • 5
    Electronic Resource
    Electronic Resource
    Selective retention of secretory proteins in the yeast endoplasmic reticulum by treatment of cells with a reducing agent (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 355-370 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; protein secretion ; protein folding ; disulphide bond formation ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have used four glycoproteins as markers to study how disulfide bond formation and protein folding effect the intracellular transport of proteins in yeast. Under normal conditions, the vacuolar enzyme carboxypeptidase Y (CPY) and the secretory stress-protein hsp150 acquired disulfide bonds in the endoplasmic reticulum (ER). Treatment of living cells with the reducing agent dithiothreitol (DTT) prevented disulfide formation of newly synthesized CPY and hsp150, resulting in retention of the proteins in the ER. When DTT was removed, the sulfhydryls were reoxidized, and the transport of the proteins to their correct destinations was resumed. Even mature CPY, located in the vacuole, could be reduced with DTT, and reoxidized after removal of the drug. DTT treatment blocked intracellular transport of hsp150 only when present during the synthesis and translocation of the protein. Reduction of folded hsp150, accumulated in the ER due to a sec block prior to DTT treatment, did not inhibit its secretion. The Kar2p/BiP protein, a component of the ER lumen, was found to be associated with fully translocated reduced hsp150, but not with native hsp150, suggesting that Kar2p/BiP may be involved in the putative retention mechanism. The cysteine-free pro-α-factor, and invertase which was shown to have free sulfhydryls, were secreted and modified similarly in the presence and absence of DTT, showing that the secretory pathway of yeast functioned under reducing conditions.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320100308
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  • 6
    Electronic Resource
    Electronic Resource
    Structural features of a polypeptide carrier promoting secretion of a β-lactamase fusion protein in yeast (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 11 (1995), S. 1381-1391 
    Details
    ISSN: 0749-503X
    Keywords: secretion ; yeast ; glycosylation ; β-lactamase ; fusion protein ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Escherichia coli β-lactamase was secreted into the culture medium of Saccharomyces cerevisiae in biologically active form, when fused to the C-terminus of the hsp150δ-carrier. The hsp150δ-carrier is an N-terminal fragment of the yeast hsp150 protein, having a signal peptide and consisting mostly of a 19 amino acid peptide repeated 11 times in tandem. Here we expressed the hsp150δ-carrier fragment alone in S. cerevisiae. Apparently due to a positional effect of the gene insertion, large amounts of the hsp150δ-carrier were synthesized. About half of the de novo synthesized carrier molecules were secreted into the culture medium, the rest remaining mostly in the pre-Golgi compartment. The extensively O-glycosylated carrier fragment was purified from the culture medium under non-denaturing conditions. Circular dichroism spectroscopy showed that it had no regular secondary structure. Nuclear magnetic resonance spectroscopy showed that a non-glycosylated synthetic peptide, the consensus sequence of the repetitive 19 amino acid peptide, also lacked secondary structure. The unstructured carrier polypeptide may facilitate proper folding and secretion of heterologous proteins attached to it.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320111406
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  • 7
    Electronic Resource
    Electronic Resource
    The hsp150Δ-carrier confers secretion competence to the rat nerve growth factor receptor ectodomain in Saccharomyces cerevisiae (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 457-466 
    Details
    ISSN: 0749-503X
    Keywords: yeast ; NGFR ; secretion ; protein production ; hsp150 protein ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: When the extracellular domain of rat low-affinity nerve growth factor receptor (NGFRe) was synthesized in Saccharomyces cerevisiae with the signal peptide of invertase, NGFRe was translocated to the endoplasmic reticulum (ER) and retained there. However, when NGFRe was fused to the C-terminus of the hsp150Δ-carrier, the hsp150Δ-NGFRe fusion protein was efficiently secreted to the growth medium with no apparent retention in the ER. The NGFRe portion was disulphide-bonded and its single N-glycosylation site was occupied. The hsp150Δ-carrier is an N-terminal signal peptide-containing fragment of a yeast secretory glycoprotein. Hsp150Δ-NGFRe, harvested from the culture medium, inhibited the cross-linking of [125I]NGF to authentic NGFR on the surface of human melanoma cells. Moreover, [125I]NGF could be chemically cross-linked to secretory hsp150Δ-NGFRe, suggesting that the NGFRe portion had adopted a ligand-binding conformation. However, inhibition of the cross-linking by unlabelled NGF was less effective than in the case of the authentic receptor. The hsp150Δ-carrier may have potential in the production of mammalian proteins, which require elaborate folding and disulphide formation in the ER.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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