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  • 1
    Electronic Resource
    Electronic Resource
    Multiple responses to heat stress by the basidiomyceteSchizophyllum commune (1993)
    Springer
    Current microbiology 26 (1993), S. 123-127 
    Details
    ISSN: 1432-0991
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Temperatures in excess of 45°C are required to stop the growth ofSchizophyllum commune colonies. Transfer of colonies from normal growth conditions (21°C) to 55°C, while halting mycelial expansion and increasing the production of aerial hyphae, was not lethal. Shortterm heat shock (3h) resulted in the appearance of nine proteins resolvable by SDS-PAGE that were newly synthesized or had their synthesis increased. The molecular weights of these proteins qualify two of them as being members of the hsp90 and hsp 70 families of heat shock proteins. Heat shock also affected proteolytic processes in the colonies. Changes in the pattern of ubiquitinated protein conjugates occurred; fewer high-molecular-weight conjugates were found in heat-shocked colonies, and the appearance of a ladder of lower-molecular-weight conjugates was noted. Protease enzymes detected by gelatin-gel PAGE showed a general decrease in activity. One of these proteases, which was up-regulated during nitrogen deprivation, showed an intermediate response during the combined stresses of heat shock and nitrogen starvation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01577364
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Proteolysis and amino acid recycling during nitrogen deprivation inSchizophyllum commune (1991)
    Springer
    Current microbiology 23 (1991), S. 27-32 
    Details
    ISSN: 1432-0991
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Transfer of exponentially growing colonies ofSchizophyllum commune to nitrogen-deficient media for 6–60 h resulted in increased general proteolytic activity and decreased extractable protein when compared with controls. A concomitant increase in free radiolabeled leucine was detected in nitrogen-deprived colonies. Radiolabel was found in new surface hyphae following transfer of previously labeled colonies to media containing no label. The concentration of label present in the new growth indicates that this label is likely to have originated from proteolytic release of label from proteins in the older, central portions of the colony. The release of substantial amounts of label into the growth medium suggests that an extra-mycelial pathway may account, at least in part, for translocation of amino acids released by proteolysis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02092305
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Two Fluorescent Markers Identify the Vacuolar System of Schizophyllum commune (1999)
    Springer
    Current microbiology 38 (1999), S. 295-299 
    Details
    ISSN: 1432-0991
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Vacuole-mediated proteolysis is important to sustained growth of filamentous wood-decaying fungi such as Schizophyllum commune. Demonstrating that specific proteases are vacuole associated has been difficult in these organisms due to the lack of specific markers for vacuolar compartments. We used 5-(and 6-)-carboxy-2′, 7′-dichlorofluorescein diacetate (carboxy-DCFDA) and a proprietary vacuolar membrane marker for yeast (MDY-64; Molecular Probes) for in situ fluorescent labeling of the vacuoles of S. commune mycelia grown on microscope slides. MDY-64 labels numerous small vesicles in S. commune mycelia in addition to larger vacuolar structures. In contrast, carboxy-DCFDA apparently is taken up by a subset of the MDY-64-labeled vesicles, accumulating primarily in larger vacuoles. Staining of mycelia with carboxy-DCFDA shows a transition from mostly cytoplasmic fluorescence in apical cells with little vacuolar fluorescence to nearly complete sequestration of the stain in vacuoles of older cells. In penultimate cells, both cytoplasm and vacuolar structures fluoresce. Vacuoles stained with carboxy-DCFDA typically were spherical and ranged in size from 0.4 μm to 3.2 μm in diameter with a mean of 1.8 um. Occasionally, in penultimate cells, tubular structures which stained with carboxy-DCFDA were found. ScPrB, a principal enzyme of nitrogen-limitation induced autolysis in S. commune, copurified in sucrose density gradients with carboxy-DCFDA and acid phosphatase, demonstrating its vacuolar localization.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/PL00006805
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  • 4
    Electronic Resource
    Electronic Resource
    Quantitative analysis of Schizophyllum commune metalloprotease ScPrB activity in SDS-gelatin PAGE reveals differential mycelial localization of nitrogen limitation-induced autolysis (1995)
    Springer
    Current microbiology 30 (1995), S. 337-343 
    Details
    ISSN: 1432-0991
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The basidiomycete Schizophyllum commune produces a variety of proteolytic enzymes. A number of these, detected in native gelatin-containing polyacrylamide gels, have their activities increased during nitrogen-limited growth of the mycelium. ScPrB, a metallo-endoprotease, appears to have the greatest nitrogen stress-induced increase in activity of all of these enzymes. Quantifying ScPrB has proven difficult because no artificial chromogenic substrate has been found. In addition, it is poorly resolved from another highly active protease, ScPrA, in native gelatin-containing gels. We have developed a method using SDS gelatin-containing polyacrylamide gels for resolving ScPrB from ScPrA and for quantifying its activity by densitometry. This method was used to assess the intramycelial location of ScPrB induction after the transfer of exponentially growing colonies to nitrogen deprivation conditions. By all analyses (proportional, normalized to fresh weight, and normalized to protein), the increase in ScPrB activity was found to occur exclusively in midsections of the growing mycelium, whereas ScPrB activity was found to be decreased or unchanged in the centers of colonies and in colony margins. This implies that proteolysis mediated by ScPrB may supply translocatable amino acids only from the region directly behind the growing hyphal apices.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00369860
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    Paper (German National Licenses)
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