Proteomic alterations induced by ionic liquids in Aspergillus nidulans and Neurospora crassa

2013 ◽  
Vol 94 ◽  
pp. 262-278 ◽  
Author(s):  
Isabel Martins ◽  
Diego O. Hartmann ◽  
Paula C. Alves ◽  
Sébastien Planchon ◽  
Jenny Renaut ◽  
...  
Keyword(s):  
Ionic Liquids ◽  
Neurospora Crassa ◽  
Aspergillus Nidulans

scholarly journals Purification of arginase from Aspergillus nidulans.

1994 ◽  
Vol 41 (4) ◽  
pp. 467-471 ◽  
Author(s):  
A Dzikowska ◽  
J P Le Caer ◽  
P Jonczyk ◽  
P Wëgleński
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Neurospora Crassa ◽  
Molecular Mass ◽  
Nitrogen Source ◽  
Aspergillus Nidulans ◽  
Sole Nitrogen Source ◽  
Mass Ratio ◽  
Conserved Domains ◽  
Native Molecular Mass ◽  
High Degree

Arginase (EC 3.5.3.1) of Aspergillus nidulans, the enzyme which enables the fungus to use arginine as the sole nitrogen source was purified to homogeneity. Molecular mass of the purified arginase subunit is 40 kDa and is similar to that reported for the Neurospora crassa (38.3 kDa) and Saccharomyces cerevisiae (39 kDa) enzymes. The native molecular mass of arginase is 125 kDa. The subunit/native molecular mass ratio suggests a trimeric form of the protein. The arginase protein was cleaved and partially sequenced. Two out of the six polypeptides sequenced show a high degree of homology to conserved domains in arginases from other species.

scholarly journals Cellular and extracellular siderophores of Aspergillus nidulans and Penicillium chrysogenum.

1981 ◽  
Vol 1 (2) ◽  
pp. 94-100 ◽  
Author(s):  
G Charlang ◽  
B Ng ◽  
N H Horowitz ◽  
R M Horowitz
Keyword(s):  
Biological Activity ◽  
Neurospora Crassa ◽  
Aspergillus Nidulans ◽  
Water Activity ◽  
Penicillium Chrysogenum ◽  
Mycelial Growth ◽  
Culture Medium ◽  
Highly Active ◽  
Assay Procedure ◽  
Generally True

Aspergillus nidulans and Penicillium chrysogenum produce specific cellular siderophores in addition to the well-known siderophores of the culture medium. Since this was found previously in Neurospora crassa, it is probably generally true for filamentous ascomycetes. The cellular siderophore of A. nidulans is ferricrocin; that of P. chrysogenum is ferrichrome. A. nidulans also contains triacetylfusigen, a siderophore without apparent biological activity. Conidia of both species lose siderophores at high salt concentrations and become siderophore dependent. This has also been found in N. crassa, where lowering of the water activity has been shown to be the causal factor. We used an assay procedure based on this dependency to reexamine the extracellular siderophores of these species. During rapid mycelial growth, both A. nidulans and P. chrysogenum produced two highly active, unidentified siderophores which were later replaced by a less active or inactive product--coprogen in the case of P. chrysogenum and triacetylfusigen in the case of A. nidulans. N. crassa secreted coprogen only. Fungal siderophore metabolism is varied and complex.

acon-3, the Neurospora crassa ortholog of the developmental modifier, medA, complements the conidiation defect of the Aspergillus nidulans mutant

2011 ◽  
Vol 48 (4) ◽  
pp. 370-376 ◽  
Author(s):  
Da-Woon Chung ◽  
Charles Greenwald ◽  
Srijana Upadhyay ◽  
Shengli Ding ◽  
Heather H. Wilkinson ◽  
...  
Keyword(s):  
Neurospora Crassa ◽  
Aspergillus Nidulans

scholarly journals CYTOCHEMICAL DETECTION OF HYDROLASES IN FUNGUS CELLS III. ARYL SULFATASE

1974 ◽  
Vol 22 (3) ◽  
pp. 183-188 ◽  
Author(s):  
JÜRGEN REISS
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Enzyme Activity ◽  
Neurospora Crassa ◽  
Aspergillus Nidulans ◽  
Aspergillus Oryzae ◽  
Coupling Agent ◽  
Mycelial Fungi ◽  
Aryl Sulfatase ◽  
Negative Results ◽  
Coupling Procedure

In the cells of Aspergillus oryzae, Aspergillus nidulans, Neurospora crassa and Saccharomyces cerevisiae, aryl sulfatase can be demonstrated by incubation in a medium containing 6-bromo-2-naphthylsulfate as substrate and fast garnet GBC as coupling agent. Controls confirm the specificity of the reaction. Other incubation solutions (two Gomori media and a simultaneous coupling procedure with 8-hydroxyquinoline sulfate as substrate) gave negative results or reaction pictures equally to those in substrate-free control. The possible reasons for this are discussed. In the mycelial fungi the strongest enzyme activity is located in the most intensely metabolizing parts: tips of the hyphae and the differentiating parts of the conidiophores. The reaction granules in all four fungi are possibly identical with lysosomes.

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