Regulation of mannitol-1-phosphate dehydrogenase in Aspergillus nidulans

1975 ◽  
Vol 21 (1) ◽  
pp. 99-101 ◽  
Author(s):  
Oliver Hankinson ◽  
David J. Cove

When Aspergillus nidulans is grown with urea as sole nitrogen source it possesses about sixtold higher activity of mannitol-1-phosphate dehydrogenase than when it is grown with both urea and sodium nitrate.

1994 ◽  
Vol 41 (4) ◽  
pp. 467-471 ◽  
Author(s):  
A Dzikowska ◽  
J P Le Caer ◽  
P Jonczyk ◽  
P Wëgleński

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.


1960 ◽  
Vol 38 (4) ◽  
pp. 613-622 ◽  
Author(s):  
Kaiser Naguib ◽  
Kamel Saddik

Aspergillus nidulans has been grown in surface culture on high-sugar media favorable for fat formation and containing, as nitrogen source, sodium nitrate, ammonium chloride, or asparagine. Growth, sugar and nitrogen uptake, and syntheses of carbohydrates, proteins, and fat were all followed over an incubation period of 20 days. In the early stages, growth was influenced by the nature of the nitrogen source, being highest on asparagine and lowest on ammonium chloride, with the same sugar uptake. Later, dry weight increase proceeded at a high rate on asparagine, at a moderate rate on sodium nitrate, and it almost stopped on ammonium chloride, where the pH dropped to a very low value. At this stage, increase in dry weight followed sugar absorption, and was due to accretion of non-nitrogenous compounds.Asparagine media were by far superior to nitrate or ammonium media for fat formation. Protein and carbohydrate contents were higher in nitrate- than in asparagine- or ammonium-fed mycelial felts. All synthetic processes almost stopped in ammonium cultures after the early growth phase. It seems that the attitude of the fungus towards ammonium nitrogen could not be fully manifested due to restricted growth, and therefore it is suggested that no definite conclusions with regard to ammonium utilization by Aspergillus nidulans can be drawn unless the pH of the medium is controlled and growth on ammonium nitrogen made possible.


1975 ◽  
Vol 21 (6) ◽  
pp. 807-810 ◽  
Author(s):  
J. D. Desai ◽  
V. V. Modi

A marked increase in the cellular synthesis accompanied by a decrease in the total fatty acid content was observed when Aspergillus nidulans was grown on NH4NO3 as a sole nitrogen source, in the medium containing avidin. Because of the increased uptake of NH4+, the level of NH4+ was lowered in the medium; as a result there is early uptake and assimilation of nitrate by a biotin-deficient culture as compared with the normal culture of A. nidulans. At about 17 mM concentration, NH4+ repressed the activity of nitrate reductase. The regulation of NO3− uptake and its assimilation with respect to the growth of A. nidulans have been discussed.


1953 ◽  
Vol 31 (1) ◽  
pp. 28-32 ◽  
Author(s):  
A. C. Blackwood

One hundred and fourteen bacterial cultures representing most of the species in the Bacillus genus were tested for the production of extracellular barley gum cytase. Assays were made on shake-flask cultures grown on a medium containing glucose and yeast extract. Although all the organisms had some enzymatic activity, certain strains of Bacillus subtilis gave the best yields of cytase. On a medium with asparagine as the sole nitrogen source even higher yields were obtained. The crude cytase preparations were stable and after freeze-drying most of the original activity remained.


1975 ◽  
Vol 28 (3) ◽  
pp. 301 ◽  
Author(s):  
MJ Hynes

Mutants of Apergillus nidulanswith lesions in a gene, areA (formerly called amdT), have been isolated by a variety of different selection methods. The areA mutants show a range of pleiotropic growth responses to a number of compounds as sole nitrogen sources, but are normal in utilization of carbon sources. The levels of two amidase enzymes as well as urease have been investigated in the mutants and have been shown to be affected by this gene. Most of the areA mutants have much lower amidase-specific activities when grown in ammonium-containing medium, compared with mycelium incubated in medium la9king a nitrogen source. Some of the areA. mutants do not show derepression of urease upon relief of ammonium repression. The dominance relationships of areA alleles have been investigated in� heterozygous diploids, and these studies lend support to the proposal that areA codes for a positively acting regulatory product. One of the new areA alleles is partially dominant to areA + and areA102. This may be a result of negative complementation or indicate that areA has an additional negative reiuIatory function. Investigation.of various amdR; areA double mutants has led to the conclusion that amdR and areA participate in independent regulatory circuits in the control of acetamide utilizatiol1. Studies on an amdRc; areA.double mutant indicate that areA is involved in derepression of acetamidase upon relief of ammo.nium repression.


2010 ◽  
Vol 76 (12) ◽  
pp. 4102-4104 ◽  
Author(s):  
Yin Chen ◽  
Kathryn L. McAleer ◽  
J. Colin Murrell

ABSTRACT Monomethylamine can be used by nonmethylotrophs as a sole nitrogen source but not as a carbon source; however, little is known about the genes and enzymes involved. The γ-glutamylmethylamide/N-methylglutamate pathway for monomethylamine utilization by methylotrophs has recently been resolved. We have identified genes encoding key enzymes of this pathway in nonmethylotrophs (e.g., Agrobacterium tumefaciens) and demonstrated that this pathway is also involved in the utilization of monomethylamine as a nitrogen source by nonmethylotrophs.


1975 ◽  
Vol 25 (2) ◽  
pp. 119-135 ◽  
Author(s):  
Meryl Polkinghorne ◽  
M. J. Hynes

SUMMARYWild-type strains ofAspergillus nidulansgrow poorly onL-histidine as a sole nitrogen source. The synthesis of the enzyme histidase (EC. 4.3.1.3) appears to be a limiting factor in the growth of the wild type, as strains carrying the mutantareA102 allele have elevated histidase levels and grow strongly on histidine as a sole nitrogen source.L-Histidine is an extremely weak sole carbon source for all strains.Ammonium repression has an important role in the regulation of histidase synthesis and the relief of ammonium repression is dependent on the availability of a good carbon source. The level of histidase synthesis does not respond to the addition of exogenous substrate.Mutants carrying lesions in thesarA orsarB loci (suppressor ofareA102) have been isolated. The growth properties of these mutants on histidine as a sole nitrogen source correlate with the levels of histidase synthesized. Mutation at thesarA andsarB loci also reduces the utilization of a number of other nitrogen sources. The data suggest that these two genes may code for regulatory products involved in nitrogen catabolism. No histidase structural gene mutants were identified and possible explanations of this are discussed.


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