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  • 1
    Electronic Resource
    Electronic Resource
    Circadian Oscillation in Rat Liver Tryptophan Pyrrolase and its Analysis by Substrate and Hormone Induction (1968)
    [s.l.] : Nature Publishing Group
    Nature 219 (1968), S. 619-621 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Male Sprague-Dawley rats, 4?6 months old and weighing 260?360 g, were kept under a light-dark cycle of 12 : 12 h. At eight different times of day, three to five rats were killed and the livers were excised and homogenized in a cold solution of 0.14 M KC1 containing 0.0025 N NaOH. The homogenates ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/219619a0
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  • 2
    Electronic Resource
    Electronic Resource
    Interaction of the Neurospora crassa heat shock factor with the heat shock element during heat shock and different developmental stages (2000)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 185 (2000), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The interaction of the heat shock factor (HSF) with the heat shock element (HSE) was determined by a non-radioactive electrophoretic mobility shift assay, in order to analyze HSF regulation in Neurospora crassa. HSF binds to HSE under normal, non-stress conditions and is thus constitutively trimerized. Upon heat shock, the HSF–HSE complex shows a retarded mobility. This was also observed in Saccharomyces cerevisiae, where this mobility shift was shown to be due to HSF phosphorylation [Sorger and Pelham (1988) Cell 54, 855–864]. In N. crassa, HSE-dependent electrophoretic mobility shift is temperature- and time-dependent. Under normal growth conditions, the HSF is located in the cytoplasm as well as in the nucleus. In germinating conidia the HSF shows a retarded mobility typical for heat shock even at normal growth temperatures. No HSF-dependent mobility shift was detectable in aerial hyphae.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2000.tb09071.x
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  • 3
    Electronic Resource
    Electronic Resource
    A non-stop antisense reading frame in the grp78 gene of Neurospora crassa is homologous to the Achlya klebsiana NAD-gdh gene but is not being transcribed (2000)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 183 (2000), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: A long non-stop reading frame exists on the antisense strand of the grp78 gene (cDNA and genomic DNA) of Neurospora crassa. Computer analysis revealed a strong similarity of the putative antisense protein to the 10th exon of the NAD-dependent glutamate dehydrogenase gene (NAD-gdh) of Achlya klebsiana, which is itself located on the complementary strand of a transcribed hsc70 gene homologue. In Neurospora, no grp78 antisense mRNA was detected by Northern blot and reverse transcription-coupled polymerase chain reaction analyses, indicating that this long reading frame is not being transcribed. Hypotheses for the presence of such unexpressed non-stop reading frames are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2000.tb08976.x
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  • 4
    Electronic Resource
    Electronic Resource
    Differential stress gene expression during the development of Neurospora crassa and other fungi (1998)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 168 (1998), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Stress genes are differentially expressed during the development of Neurospora crassa and other fungi. Large amounts of constitutive heat shock protein 70 (HSC70) are found in dormant conidia of N. crassa, whereas little mRNA of the related glucose-regulated protein (grp78) is detected. It is, however, not generally clear whether heat shock protein or mRNA is preferentially stored in dormant spores. Germinating spores of N. crassa increase the level of grp mRNA. During this developmental stage, the induction of inducible heat shock protein (hsp) genes can be elicited by heat shock only at certain times after the beginning of germination. Exponential growth (proliferation) is paralleled by increased levels of HSCs. The stationary state is characterized by decreased levels of some HSCs and increased levels of others. Conidiation in N. crassa is accompanied by a strong enhancement of the synthesis and levels of HSCs but also of HSPs after heat shock. This increase may serve a need for additional rounds of replication, for the expression and transport of sporulation-specific proteins or for stabilization of macromolecules in the spores and their preservation for germination. The control mechanisms involved in the differential expression of hsc genes are currently not known.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1998.tb13268.x
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  • 5
    Electronic Resource
    Electronic Resource
    Changes in cell morphology and actin organization during heat shock in Dictyostelium discoideum: does HSP70 play a role in acquired thermotolerance? (1999)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 178 (1999), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: In response to heat shock (34°C, 30 min), cell morphology and actin organization in Dictyostelium discoideum are drastically changed. Loss of pseudopodia and disappearance of F-actin-containing structures were observed by using fluorescence microscopy. These changes were paralleled by a rapid decrease of the F-actin content measured by a TRITC-phalloidin binding assay. The effects of heat shock on cell morphology and actin organization are transient: After heat shock (34°C) or during a long-term heat treatment (30°C), cell morphology, F-actin patterns and F-actin content recovered/adapted to a state which is characteristic for untreated cells. Because F-actin may be stabilized by increased amounts of heat shock proteins, their response and interaction with F-actin was analyzed. After a 1 h heat treatment (34°C), the major heat shock protein of D. discoideum (HSP70) showed maximally increased synthesis rates and levels. During recovery from a 34°C shock or during a continuous heat treatment at 30°C, the HSP70 content first increased and then declined slowly toward normal levels. Pre-treatment of cells with a short heat shock of 30 min at 34°C stabilized the F-actin content when the cells were exposed to a second heat shock. Furthermore, a transient colocalization of HSP70 and actin was observed at the beginning of heat treatment (30°C) using immunological detection of HSP70 in the cytoskeletal actin fraction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1999.tb13764.x
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  • 6
    Electronic Resource
    Electronic Resource
    Nuclear translocation of constitutive heat shock protein 70 during S phase in synchronous macroplasmodia of Physarum polycephalum (1997)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 152 (1997), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The level of constitutive heat shock protein 70 (HSC70) in Physarum polycephalum was analyzed by means of Western blots during the synchronous cell cycle of macroplasmodia. Total amounts as well as nuclear and cytoplasmic contents were determined separately and evaluated densitometrically. A drastic increase of nuclear HSC70 was observed 10–40 min after the initiation of S phase (600% of the M phase value) and thereafter a slow decline toward the next M phase. Total HSC levels showed a slight (30%) increase during S phase whereas cytoplasmic HSC70 was about 30% lower during S phase compared to mitosis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1997.tb10413.x
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  • 7
    Electronic Resource
    Electronic Resource
    Heat shock inhibits and activates different protein degradation pathways and proteinase activities in Neurospora crassa (1994)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 124 (1994), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract In Neurospora crassa, heat shock treatment inhibits proteolytic activity. ATP-independent proteinases were analysed after polyacrylamide gel electrophoresis using renaturing gelatine gels. Proteinases of 24, 29, and 130 kDa were shown to be inhibited by heat shock and were further characterized as to their properties. A major part of the heat shock-induced inhibition is probably due to suppression of de novo synthesis of proteinases as deduced from experiments with cycloheximide. During several hours of recovery from heat shock, the inhibition of overall protein degradation and ATP-independent proteinases is reversed. Azocasein assays as well as pulse-chase experiments further showed that ATP-dependent protein degradation is only slightly affected by heat shock. Two ATP-binding proteinases of about 60 and 160 kDa even show an increased activity after heat shock. The degradation rate of heat shock proteins is inhibited by heat shock treatment, indicating that they are degraded by ATP-independent proteinases. Western blot analysis of a ∼40-kDa degradation product of HSP70 containing its amino terminal portion revealed a reduction in the amount of this peptide after heat shock.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1994.tb07287.x
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  • 8
    Electronic Resource
    Electronic Resource
    Streßproteine: Ihre wachsende Bedeutung in der Medizin (1995)
    Springer
    Naturwissenschaften 82 (1995), S. 303-309 
    Details
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01131526
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  • 9
    Electronic Resource
    Electronic Resource
    Streßproteine: Ihre wachsende Bedeutung in der Medizin (1995)
    Springer
    Naturwissenschaften 82 (1995), S. 303-309 
    Details
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01131526
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  • 10
    Electronic Resource
    Electronic Resource
    Circadian changes in protein-synthesis rate and protein phosphorylation in cell-free extracts of Gonyaulax polyedra (1987)
    Springer
    Planta 170 (1987), S. 7-13 
    Details
    ISSN: 1432-2048
    Keywords: Circadian rhythm ; Gonyaulax ; Protein phosphorylation ; Protein synthesis (cell free)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The polysomal pattern of the dinoflagellate Gonyaulax polyedra, cultured under constant conditions, demonstrates a circadian rhythm. The relative amount of polysomes increases during the phase corresponding to the previous night period (=subjective night phase) when the rate of protein synthesis reaches its maximum (Cornelius et al., 1985, Planta 160, 365–370). Cell-free extracts were isolated at different circadian phase. The rate of protein synthesis in the extracts changed rhythmically in the same manner as the rate of protein synthesis in vivo. Substances in the postribosomal supernatants influenced the protein-synthesis rate of the cell-free system, depending on the phase when they were isolated: “night factors” stimulated protein synthesis in “day extracts” whereas “day factors” inhibited protein synthesis in “night extracts”. These effects were abolished by heating the postribosomal supernatant. In-vitro phosphorylation in parallel probes showed changes in the pattern of phosphorylated proteins. Phosphorylation of one of the proteins (95 kDa) was decreased after addition of “night factor(s)” and increased after addition of “day factor(s)”. Cyclic-AMP enhanced the rates of protein synthesis and phosphorylation in the day extracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00392374
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