Characterization of melanin pigment produced by Aspergillus nidulans

2011 ◽  
Vol 28 (4) ◽  
pp. 1467-1474 ◽  
Author(s):  
R. C. R. Gonçalves ◽  
H. C. F. Lisboa ◽  
S. R. Pombeiro-Sponchiado
Keyword(s):  
Aspergillus Nidulans ◽  
Melanin Pigment

Characterization of the Role of the FluG Protein in Asexual Development of Aspergillus nidulans

Genetics ◽  
2001 ◽  
Vol 158 (3) ◽  
pp. 1027-1036 ◽  
Author(s):  
Cletus A D'Souza ◽  
Bee Na Lee ◽  
Thomas H Adams
Keyword(s):  
Aspergillus Nidulans ◽  
Negative Influence ◽  
Asexual Development ◽  
Wild Type ◽  
Significant Similarity ◽  
Developmental Defects ◽  
Asexual Sporulation ◽  
Type Strains

Abstract We showed previously that a ΔfluG mutation results in a block in Aspergillus nidulans asexual sporulation and that overexpression of fluG activates sporulation in liquid-submerged culture, a condition that does not normally support sporulation of wild-type strains. Here we demonstrate that the entire N-terminal region of FluG (∼400 amino acids) can be deleted without affecting sporulation, indicating that FluG activity resides in the C-terminal half of the protein, which bears significant similarity with GSI-type glutamine synthetases. While FluG has no apparent role in glutamine biosynthesis, we propose that it has an enzymatic role in sporulation factor production. We also describe the isolation of dominant suppressors of ΔfluG(dsg) that should identify components acting downstream of FluG and thereby define the function of FluG in sporulation. The dsgA1 mutation also suppresses the developmental defects resulting from ΔflbA and dominant activating fadA mutations, which both cause constitutive induction of the mycelial proliferation pathway. However, dsgA1 does not suppress the negative influence of these mutations on production of the aflatoxin precursor, sterigmatocystin, indicating that dsgA1 is specific for asexual development. Taken together, our studies define dsgA as a novel component of the asexual sporulation pathway.

scholarly journals Structural and functional characterization of a highly secreted α- l -arabinofuranosidase (GH62) from Aspergillus nidulans grown on sugarcane bagasse

2017 ◽  
Vol 1865 (12) ◽  
pp. 1758-1769 ◽  
Author(s):  
Fabiano Jares Contesini ◽  
Marcelo Vizoná Liberato ◽  
Marcelo Ventura Rubio ◽  
Felipe Calzado ◽  
Mariane Paludetti Zubieta ◽  
...  
Keyword(s):  
Aspergillus Nidulans ◽  
Sugarcane Bagasse ◽  
Functional Characterization

scholarly journals Comparative studies on O-acetylhomoserine sulfhydrylase: physiological role and characterization of the Aspergillus nidulans enzyme.

1993 ◽  
Vol 40 (3) ◽  
pp. 421-428 ◽  
Author(s):  
J Brzywczy ◽  
S Yamagata ◽  
A Paszewski
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Substrate Specificity ◽  
Aspergillus Nidulans ◽  
Comparative Studies ◽  
Alternative Pathway ◽  
Physiological Role ◽  
Oligomeric Protein ◽  
Cysteine Synthesis ◽  
Sulfhydryl Compounds

O-acetylhomoserine sulfhydrylase (OAH SHLase) from Aspergillus nidulans is an oligomeric protein with a broad substrate specificity with regard to sulfhydryl compounds. As its Saccharomyces cerevisiae counterpart the enzyme also reacts with O-acetylserine and is inhibited by carbonyl reagents but not by antiserum raised against the yeast enzyme. In contrast to Saccharomyces cerevisiae the enzyme is not essential for Aspergillus nidulans as indicated by the completely prototrophic phenotype of OAH SHLase-negative mutants. Its major physiological role in Aspergillus nidulans seems to be recycling of the thiomethyl group of methylthio-adenosine but it is also a constituent of the alternative pathway of cysteine synthesis.

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