Regulation of Extracellular Proteinase Production in an Ectomycorrhizal Fungus Hebeloma crustuliniforme

Mycologia ◽  
1994 ◽  
Vol 86 (2) ◽  
pp. 227 ◽  
Author(s):  
Hong Zhu ◽  
Bruce P. Dancik ◽  
Kenneth O. Higginbotham
1986 ◽  
Vol 64 (11) ◽  
pp. 2753-2757 ◽  
Author(s):  
A. Tyminska ◽  
F. Le Tacon ◽  
J. Chadoeuf

The objective of this study was to determine the different effects of three ectomycorrhizal fungi (Laccaria laccata, Hebeloma crustuliniforme, and Thelephora terrestris) on the growth and mineral nutrition of Pinus silvestris at different levels of soluble phosphorus. Even a low intensity of infection by Laccaria laccata stimulated Pinus silvestris growth greatly. The ability of this ectomycorrhizal fungus to increase Pinus silvestris growth seemed to be more related to its capacity to produce growth substances than to its capacity to stimulate phosphorus uptake. The poor efficiency of Hebeloma crustuliniforme compared with Laccaria laccata at any level of phosphorus could result from differences in diversion of carbohydrates from the host to fungal structures.


Mycologia ◽  
1994 ◽  
Vol 86 (2) ◽  
pp. 227-234 ◽  
Author(s):  
Hong Zhu ◽  
Bruce P. Dancik ◽  
Kenneth O. Higginbotham

1989 ◽  
Vol 281 (1) ◽  
pp. 78-80 ◽  
Author(s):  
R. Tsuboi ◽  
T. Yamaguchi ◽  
K. Matsuda ◽  
H. Ogawa

1985 ◽  
Vol 52 (1) ◽  
pp. 91-100 ◽  
Author(s):  
Robin C. Mckeller ◽  
Hilaire Cholette

SUMMARYThe effect of chelating agents on extracellular proteinase production byPseudomonas fluorescens32A was examined. Increasing concentrations of orthophosphate slightly stimulated growth while inhibiting proteinase synthesis. Fifty percent inhibition was found at 35 and 28 mM-orthophosphate at 5 and 20 °C respectively. Extracellular protein concentration was reduced by 30% when cells were grown with 100 mM-orthophosphate. Polyacrylamide gel electrophoresis of the cell-free supernatants suggested that reduced enzyme synthesis had taken place as evidenced by the decrease in staining intensity of the protein band corresponding to the proteinase. Other phosphate compounds could replace orthophosphate as an inhibitor. Extent of inhibition was related to chain length; polyphosphates with 4–6 or 13–18 phosphorus atoms were the most effective inhibitors. EDTA (0·5 mM) completely inhibited proteinase synthesis. This inhibition could be partly reversed by Ca2+and, to a lesser extent, Mn2+. Proteinase production at 5 °C in skim milk was completely inhibited by phosphate glass (P13–P18). Control experiments showed that loss of activity with chelators was not due to inhibition of preformed enzyme. The results suggest a possible role for polyphosphates in controlling proteinase production in stored milk.


Planta ◽  
1996 ◽  
Vol 198 (1) ◽  
Author(s):  
Peter Salzer ◽  
Gerhard Hebe ◽  
Andreas Reith ◽  
Barbara Zitterell-Haid ◽  
Harald Stransky ◽  
...  

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