scholarly journals On the Evidence Supporting That AN11127 Encodes an Aspergillus Nidulans Sec12 Orthologous Protein. Reply to Bravo-Plaza et al. Comment on “Dimou et al. Profile of Membrane Cargo Trafficking Proteins and Transporters Expressed under N Source Derepressing Conditions in Aspergillus nidulans. J. Fungi 2021, 7, 560”

2021 ◽  
Vol 7 (12) ◽  
pp. 1040
Author(s):  
Sofia Dimou ◽  
Xenia Georgiou ◽  
Eleana Sarantidi ◽  
George Diallinas ◽  
Athanasios K. Anagnostopoulos
Keyword(s):  
Aspergillus Nidulans ◽  
Orthologous Protein ◽  
N Source ◽  
And Function

Prof. Peñalva and co-workers provided evidence that AN11127 is related by sequence and function to Sec12 [...]

scholarly journals Impact of Membrane Lipids on UapA and AzgA Transporter Subcellular Localization and Activity in Aspergillus nidulans

2021 ◽  
Vol 7 (7) ◽  
pp. 514
Author(s):  
Mariangela Dionysopoulou ◽  
George Diallinas
Keyword(s):  
Plasma Membrane ◽  
Subcellular Localization ◽  
Aspergillus Nidulans ◽  
Membrane Lipids ◽  
Membrane Lipid ◽  
Lipid Biosynthesis ◽  
Transport Kinetics ◽  
Negative Effect ◽  
And Function

Recent biochemical and biophysical evidence have established that membrane lipids, namely phospholipids, sphingolipids and sterols, are critical for the function of eukaryotic plasma membrane transporters. Here, we study the effect of selected membrane lipid biosynthesis mutations and of the ergosterol-related antifungal itraconazole on the subcellular localization, stability and transport kinetics of two well-studied purine transporters, UapA and AzgA, in Aspergillus nidulans. We show that genetic reduction in biosynthesis of ergosterol, sphingolipids or phosphoinositides arrest A. nidulans growth after germling formation, but solely blocks in early steps of ergosterol (Erg11) or sphingolipid (BasA) synthesis have a negative effect on plasma membrane (PM) localization and stability of transporters before growth arrest. Surprisingly, the fraction of UapA or AzgA that reaches the PM in lipid biosynthesis mutants is shown to conserve normal apparent transport kinetics. We further show that turnover of UapA, which is the transporter mostly sensitive to membrane lipid content modification, occurs during its trafficking and by enhanced endocytosis, and is partly dependent on autophagy and Hect-type HulARsp5 ubiquitination. Our results point out that the role of specific membrane lipids on transporter biogenesis and function in vivo is complex, combinatorial and transporter-dependent.

scholarly journals The splicing-factor Prp40 affects dynein–dynactin function in Aspergillus nidulans

2020 ◽  
Vol 31 (12) ◽  
pp. 1289-1301 ◽  
Author(s):  
Rongde Qiu ◽  
Jun Zhang ◽  
Xin Xiang
Keyword(s):  
Aspergillus Nidulans ◽  
Early Endosome ◽  
Splicing Factor ◽  
Factors Affecting ◽  
Mutant Screen ◽  
And Function

We performed a genomewide mutant screen for genes affecting dynein-mediated early-endosome distribution in Aspergillus nidulans, and we unexpectedly identified Prp40A, a homologue of the yeast splicing factor Prp40. Prp40A and its higher eukaryotic homologues may represent new factors affecting the assembly and function of dynein-dynactin.

scholarly journals Suppression of the bimC4 mitotic spindle defect by deletion of klpA, a gene encoding a KAR3-related kinesin-like protein in Aspergillus nidulans.

1993 ◽  
Vol 120 (1) ◽  
pp. 153-162 ◽  
Author(s):  
M J O'Connell ◽  
P B Meluh ◽  
M D Rose ◽  
N R Morris
Keyword(s):  
Aspergillus Nidulans ◽  
Mitotic Spindle ◽  
Structural Similarity ◽  
Temperature Sensitive ◽  
Gene Encoding ◽  
Expression Studies ◽  
Primary Amino ◽  
And Function ◽  
Spindle Function ◽  
The Relationship

To investigate the relationship between structure and function of kinesin-like proteins, we have identified by polymerase chain reaction (PCR) a new kinesin-like protein in the filamentous fungus Aspergillus nidulans, which we have designated KLPA. DNA sequence analysis showed that the predicted KLPA protein contains a COOH terminal kinesin-like motor domain. Despite the structural similarity of KLPA to the KAR3 and NCD kinesin-like proteins of Saccharomyces cerevisiae and Drosophila melanogaster, which also posses COOH-terminal kinesin-like motor domains, there are no significant sequence similarities between the nonmotor or tail portions of these proteins. Nevertheless, expression studies in S. cerevisiae showed that klpA can complement a null mutation in KAR3, indicating that primary amino acid sequence conservation between the tail domains of kinesin-like proteins is not necessarily required for conserved function. Chromosomal deletion of the klpA gene exerted no observable mutant phenotype, suggesting that in A. nidulans there are likely to be other proteins functionally redundant with KLPA. Interestingly, the temperature sensitive phenotype of a mutation in another gene, bimC, which encodes a kinesin-like protein involved in mitotic spindle function in A. nidulans, was suppressed by deletion of klpA. We hypothesize that the loss of KLPA function redresses unbalanced forces within the spindle caused by mutation in bimC, and that the KLPA and BIMC kinesin-like proteins may play opposing roles in spindle function.

Conservation of structure and function of the aflatoxin regulatory gene aflR from Aspergillus nidulans and A. flavus

1996 ◽  
Vol 29 (6) ◽  
pp. 549-555 ◽  
Author(s):  
J.-H. Yu ◽  
Robert A. E. Butchko ◽  
Mary Fernandes ◽  
N. P. Keller ◽  
Thomas J. Leonard ◽  
...  
Keyword(s):  
Aspergillus Nidulans ◽  
Regulatory Gene ◽  
Structure And Function ◽  
And Function

Improved gene expression in Aspergillus nidulans

1995 ◽  
Vol 73 (S1) ◽  
pp. 876-884 ◽  
Author(s):  
William E. Hintz ◽  
Inge Kalsner ◽  
Ewa Plawinski ◽  
Zimin Guo ◽  
Peter A. Lagosky
Keyword(s):  
Gene Expression ◽  
Alcohol Dehydrogenase ◽  
Aspergillus Nidulans ◽  
Glucose Repression ◽  
Expression System ◽  
Therapeutic Proteins ◽  
Regulatory Sequences ◽  
Transcriptional Regulatory ◽  
And Function

A variety of gene expression systems have been developed that utilize the promoter and transcriptional regulatory sequences derived from carbon-catabolite repressed genes for the expression of heterologous genes. The alcA expression system of Aspergillus nidulans utilizes the promoter and regulatory sequences derived from the alcohol dehydrogenase I (alcA) gene. Expression of the alcA gene is repressed by a DNA-binding protein (CreA) in the presence of glucose and induced by ethanol under glucose-depleted conditions. One problem encountered during the expression of therapeutic proteins in A. nidulans is the coexpression of secreted proteases at the time of maximal secretion of heterologous product. To avoid the proteases we created an alcA promoter variant that is no longer sensitive to glucose repression hence could drive expression at earlier time points during the fermentation. The use of this promoter variant in the expression of recombinant interleukin-6 is discussed. A second problem encountered during the expression of high-quality human therapeutic proteins in Aspergillus is aberrant glycosylation. Lower eukaryotic systems, such as Aspergillus, tend to add highly branched mannosidic chains to heterologous secreted protein products. N-Glycans can be important for both the structure and function of specific glycoproteins, hence efforts are being made to in vivo alter the type and complexity of N-glycans substituted by A. nidulans. Key words: Aspergillus, gene expression, alcohol dehydrogenase, glycosylation.

scholarly journals Structure and function of a broad-specificity chitin deacetylase from Aspergillus nidulans FGSC A4

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Zhanliang Liu ◽  
Laurie M. Gay ◽  
Tina R. Tuveng ◽  
Jane W. Agger ◽  
Bjørge Westereng ◽  
...  
Keyword(s):  
Aspergillus Nidulans ◽  
Structure And Function ◽  
Chitin Deacetylase ◽  
And Function ◽  
Broad Specificity

scholarly journals Transporter oligomerization: form and function

2016 ◽  
Vol 44 (6) ◽  
pp. 1737-1744 ◽  
Author(s):  
Yilmaz Alguel ◽  
Alexander D. Cameron ◽  
George Diallinas ◽  
Bernadette Byrne
Keyword(s):  
Membrane Proteins ◽  
Aspergillus Nidulans ◽  
Membrane Trafficking ◽  
Transport Protein ◽  
Integral Membrane Proteins ◽  
Structural Basis ◽  
Protein Oligomerization ◽  
Form And Function ◽  
The Individual ◽  
And Function

Transporters are integral membrane proteins with central roles in the efficient movement of molecules across biological membranes. Many transporters exist as oligomers in the membrane. Depending on the individual transport protein, oligomerization can have roles in membrane trafficking, function, regulation and turnover. For example, our recent studies on UapA, a nucleobase ascorbate transporter, from Aspergillus nidulans, have revealed both that dimerization of this protein is essential for correct trafficking to the membrane and the structural basis of how one UapA protomer can affect the function of the closely associated adjacent protomer. Here, we review the roles of oligomerization in many particularly well-studied transporters and transporter families.

scholarly journals The Septin AspB in Aspergillus nidulans Forms Bars and Filaments and Plays Roles in Growth Emergence and Conidiation

2012 ◽  
Vol 11 (3) ◽  
pp. 311-323 ◽  
Author(s):  
Yainitza Hernández-Rodríguez ◽  
Susan Hastings ◽  
Michelle Momany
Keyword(s):  
Aspergillus Nidulans ◽  
Filamentous Fungi ◽  
Germ Tube ◽  
Fluorescent Protein ◽  
Early Growth ◽  
Content Type ◽  
Green Fluorescent ◽  
And Function ◽  
Cytoskeletal Elements ◽  
Germ Tubes

ABSTRACTIn yeast, septins form rings at the mother-bud neck and function as diffusion barriers. In animals, septins form filaments that can colocalize with other cytoskeletal elements. In the filamentous fungusAspergillus nidulansthere are five septin genes,aspA(an ortholog ofSaccharomyces cerevisiae CDC11),aspB(an ortholog ofS. cerevisiae CDC3),aspC(an ortholog ofS. cerevisiae CDC12),aspD(an ortholog ofS. cerevisiae CDC10), andaspE(found only in filamentous fungi). TheaspBgene was previously reported to be the most highly expressedAspergillus nidulansseptin and to be essential. Using improved gene targeting techniques, we found that deletion ofaspBis not lethal but results in delayed septation, increased emergence of germ tubes and branches, and greatly reduced conidiation. We also found that AspB-green fluorescent protein (GFP) localizes as rings and collars at septa, branches, and emerging layers of the conidiophore and as bars and filaments in conidia and hyphae. Bars are found in dormant and isotropically expanding conidia and in subapical nongrowing regions of hyphae and display fast movements. Filaments form as the germ tube emerges, localize to hyphal and branch tips, and display slower movements. All visible AspB-GFP structures are retained inΔaspDand lost inΔaspAandΔaspCstrains. Interestingly, in theΔaspEmutant, AspB-GFP rings, bars, and filaments are visible in early growth, but AspB-GFP rods and filaments disappear after septum formation. AspE orthologs are only found in filamentous fungi, suggesting that this class of septins might be required for stability of septin bars and filaments in highly polar cells.

Localization and function of calmodulin in live-cells of Aspergillus nidulans

2010 ◽  
Vol 47 (3) ◽  
pp. 268-278 ◽  
Author(s):  
Shaochun Chen ◽  
Yiju Song ◽  
Jinling Cao ◽  
Gang Wang ◽  
Hua Wei ◽  
...  
Keyword(s):  
Aspergillus Nidulans ◽  
Live Cells ◽  
And Function
Sign in / Sign up

Export Citation Format

Share Document