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.

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 Deletion ofcreBin Aspergillus oryzae Increases Secreted Hydrolytic Enzyme Activity

2013 ◽  
Vol 79 (18) ◽  
pp. 5480-5487 ◽  
Author(s):  
A. J. Hunter ◽  
T. A. Morris ◽  
B. Jin ◽  
C. P. Saint ◽  
J. M. Kelly
Keyword(s):  
Enzyme Activity ◽  
Aspergillus Nidulans ◽  
Aspergillus Oryzae ◽  
Hydrolytic Enzyme ◽  
Strain Improvement ◽  
Deubiquitinating Enzyme ◽  
Activity Levels ◽  
Content Type ◽  
Creb Deubiquitinating Enzyme ◽  
Increased Activity

ABSTRACTAspergillus oryzaehas been used in the food and beverage industry for centuries, and industrial strains have been produced by multiple rounds of selection. Targeted gene deletion technology is particularly useful for strain improvement in such strains, particularly when they do not have a well-characterized meiotic cycle. Phenotypes of anAspergillus nidulansstrain null for the CreB deubiquitinating enzyme include effects on growth and repression, including increased activity levels of various enzymes. We show thatAspergillus oryzaecontains a functional homologue of the CreB deubiquitinating enzyme and that a null strain shows increased activity levels of industrially important secreted enzymes, including cellulases, xylanases, amylases, and proteases, as well as alleviated inhibition of spore germination on glucose medium. Reverse transcription-quantitative PCR (RT-qPCR) analysis showed that the increased levels of enzyme activity in bothAspergillus nidulansandAspergillus oryzaeare mirrored at the transcript level, indicating transcriptional regulation. We report thatAspergillus oryzaeDAR3699, originally isolated from soy fermentation, has a similar phenotype to that of acreBdeletion mutant of the RIB40 strain, and it contains a mutation in thecreBgene. Collectively, the results forAspergillus oryzae,Aspergillus nidulans,Trichoderma reesei, andPenicillium decumbensshow that deletion ofcreBmay be broadly useful in diverse fungi for increasing production of a variety of enzymes.

scholarly journals High yield expression of the Neurospora crassa plasma membrane H(+)-ATPase in Saccharomyces cerevisiae

1994 ◽  
Vol 269 (26) ◽  
pp. 17705-17712
Author(s):  
S.K. Mahanty ◽  
U.S. Rao ◽  
R.A. Nicholas ◽  
G.A. Scarborough
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Plasma Membrane ◽  
Neurospora Crassa ◽  
High Yield

scholarly journals Analysis of thepdx-1(snz-1/sno-1) Region of theNeurospora crassaGenome: Correlation of Pyridoxine-Requiring Phenotypes With Mutations in Two Structural Genes

Genetics ◽  
2001 ◽  
Vol 157 (3) ◽  
pp. 1067-1075 ◽  
Author(s):  
Laura E Bean ◽  
William H Dvorachek ◽  
Edward L Braun ◽  
Allison Errett ◽  
Gregory S Saenz ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Stationary Phase ◽  
Neurospora Crassa ◽  
Vitamin B6 ◽  
Structural Genes ◽  
Protein Coding ◽  
Previous Conclusion ◽  
Protein Coding Genes ◽  
Shared Function ◽  
High Gene

AbstractWe report the analysis of a 36-kbp region of the Neurospora crassa genome, which contains homologs of two closely linked stationary phase genes, SNZ1 and SNO1, from Saccharomyces cerevisiae. Homologs of SNZ1 encode extremely highly conserved proteins that have been implicated in pyridoxine (vitamin B6) metabolism in the filamentous fungi Cercospora nicotianae and in Aspergillus nidulans. In N. crassa, SNZ and SNO homologs map to the region occupied by pdx-1 (pyridoxine requiring), a gene that has been known for several decades, but which was not sequenced previously. In this study, pyridoxine-requiring mutants of N. crassa were found to possess mutations that disrupt conserved regions in either the SNZ or SNO homolog. Previously, nearly all of these mutants were classified as pdx-1. However, one mutant with a disrupted SNO homolog was at one time designated pdx-2. It now appears appropriate to reserve the pdx-1 designation for the N. crassa SNZ homolog and pdx-2 for the SNO homolog. We further report annotation of the entire 36,030-bp region, which contains at least 12 protein coding genes, supporting a previous conclusion of high gene densities (12,000-13,000 total genes) for N. crassa. Among genes in this region other than SNZ and SNO homologs, there was no evidence of shared function. Four of the genes in this region appear to have been lost from the S. cerevisiae lineage.

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