scholarly journals The function of the three phosphoribosyl pyrophosphate synthetase (Prs) genes in hyphal growth and conidiation in Aspergillus nidulans

Microbiology ◽  
2017 ◽  
Vol 163 (2) ◽  
pp. 218-232 ◽  
Author(s):  
Ping Jiang ◽  
Wen-fan Wei ◽  
Guo-wei Zhong ◽  
Xiao-gang Zhou ◽  
Wei-ran Qiao ◽  
...  
Keyword(s):  
Aspergillus Nidulans ◽  
Hyphal Growth ◽  
Phosphoribosyl Pyrophosphate ◽  
Phosphoribosyl Pyrophosphate Synthetase

scholarly journals Aspergillus nidulans ArfB Plays a Role in Endocytosis and Polarized Growth

2008 ◽  
Vol 7 (8) ◽  
pp. 1278-1288 ◽  
Author(s):  
Soo Chan Lee ◽  
Sabrina N. Schmidtke ◽  
Lawrence J. Dangott ◽  
Brian D. Shaw
Keyword(s):  
Aspergillus Nidulans ◽  
Filamentous Fungi ◽  
Fluorescent Protein ◽  
Homo Sapiens ◽  
Hyphal Growth ◽  
Life Cycles ◽  
Small Gtpase ◽  
Polarized Growth ◽  
Sequence Alignments ◽  
Green Fluorescent

ABSTRACT Filamentous fungi undergo polarized growth throughout most of their life cycles. The Spitzenkörper is an apical organelle composed primarily of vesicles that is unique to filamentous fungi and is likely to act as a vesicle supply center for tip growth. Vesicle assembly and trafficking are therefore important for hyphal growth. ADP ribosylation factors (Arfs), a group of small GTPase proteins, play an important role in nucleating vesicle assembly. Little is known about the role of Arfs in filamentous hyphal growth. We found that Aspergillus nidulans is predicted to encode six Arf family proteins. Analysis of protein sequence alignments suggests that A. nidulans ArfB shares similarity with ARF6 of Homo sapiens and Arf3p of Saccharomyces cerevisiae. An arfB null allele (arfB disrupted by a transposon [arfB::Tn]) was characterized by extended isotropic growth of germinating conidia followed by cell lysis or multiple, random germ tube emergence, consistent with a failure to establish polarity. The mutant germ tubes and hyphae that do form initially meander abnormally off of the axis of polarity and frequently exhibit dichotomous branching at cell apices, consistent with a defect in polarity maintenance. FM4-64 staining of the arfB::Tn strain revealed that another phenotypic characteristic seen for arfB::Tn is a reduction and delay in endocytosis. ArfB is myristoylated at its N terminus. Green fluorescent protein-tagged ArfB (ArfB::GFP) localizes to the plasma membrane and endomembranes and mutation (ArfBG2A::GFP) of the N-terminal myristoylation motif disperses the protein to the cytoplasm rather than to the membranes. These results demonstrate that ArfB functions in endocytosis to play important roles in polarity establishment during isotropic growth and polarity maintenance during hyphal extension.

scholarly journals Proliferation of Intrahyphal Hyphae Caused by Disruption ofcsmA, Which Encodes a Class V Chitin Synthase with a Myosin Motor-Like Domain in Aspergillus nidulans

1999 ◽  
Vol 181 (12) ◽  
pp. 3721-3729 ◽  
Author(s):  
Hiroyuki Horiuchi ◽  
Makoto Fujiwara ◽  
Shuichi Yamashita ◽  
Akinori Ohta ◽  
Masamichi Takagi
Keyword(s):  
Cell Wall ◽  
Aspergillus Nidulans ◽  
Wild Type Strain ◽  
Hyphal Growth ◽  
Chitin Synthase ◽  
Calcofluor White ◽  
Class V ◽  
Myosin Motor ◽  
Fungal Morphogenesis ◽  
Novel Protein

ABSTRACT We have found that the Aspergillus nidulans csmA gene encodes a novel protein which consists of an N-terminal myosin motor-like domain and a C-terminal chitin synthase domain (M. Fujiwara, H. Horiuchi, A. Ohta, and M. Takagi, Biochem. Biophys. Res. Commun. 236:75–78, 1997). To clarify the roles of csmA in fungal morphogenesis, we constructed csmA null mutants. The growth rate of the mutant colonies was almost the same as that of the wild-type strain, but hyphal growth was severely inhibited when a chitin-binding reagent, Calcofluor white or Congo red, was added to the medium. Moreover, morphological abnormalities in tip growth and septum formation were identified microscopically. Proliferation of intracellular new hyphae, called intrahyphal hyphae, which behaved as intrinsic hyphae, was the most striking phenotypic feature among them. These phenotypes were not suppressed when the only chitin synthase domain of csmA was expressed under the control of thealcA promoter, whereas they were suppressed when the intact form of csmA was expressed. Therefore, it was concluded that the product of csmA (CsmA) has important roles in polarized cell wall synthesis and maintenance of cell wall integrity and that the myosin motor-like domain is indispensable for these functions.

scholarly journals Calcineurin and Calcium Channel CchA Coordinate the Salt Stress Response by Regulating Cytoplasmic Ca2+Homeostasis in Aspergillus nidulans

2016 ◽  
Vol 82 (11) ◽  
pp. 3420-3430 ◽  
Author(s):  
Sha Wang ◽  
Xiao Liu ◽  
Hui Qian ◽  
Shizhu Zhang ◽  
Ling Lu
Keyword(s):  
Salt Stress ◽  
Calcium Channel ◽  
Aspergillus Nidulans ◽  
Transient Receptor Potential ◽  
Feedback Inhibition ◽  
Calcium Influx ◽  
Hyphal Growth ◽  
Salt Stress Response ◽  
Content Type ◽  
Growth Defects

ABSTRACTThe eukaryotic calcium/calmodulin-dependent protein phosphatase calcineurin is crucial for the environmental adaption of fungi. However, the mechanism of coordinate regulation of the response to salt stress by calcineurin and the high-affinity calcium channel CchA in fungi is not well understood. Here we show that the deletion ofcchAsuppresses the hyphal growth defects caused by the loss of calcineurin under salt stress inAspergillus nidulans. Additionally, the hypersensitivity of the ΔcnaAstrain to extracellular calcium and cell-wall-damaging agents can be suppressed bycchAdeletion. Using the calcium-sensitive photoprotein aequorin to monitor the cytoplasmic Ca2+concentration ([Ca2+]c) in living cells, we found that calcineurin negatively regulates CchA on calcium uptake in response to external calcium in normally cultured cells. However, in salt-stress-pretreated cells, loss of eithercnaAorcchAsignificantly decreased the [Ca2+]c, but a deficiency in bothcnaAandcchAswitches the [Ca2+]cto the reference strain level, indicating that calcineurin and CchA synergistically coordinate calcium influx under salt stress. Moreover, real-time PCR results showed that the dysfunction ofcchAin the ΔcnaAstrain dramatically restored the expression ofenaA(a major determinant for sodium detoxification), which was abolished in the ΔcnaAstrain under salt stress. These results suggest that double deficiencies ofcnaAandcchAcould bypass the requirement of calcineurin to induceenaAexpression under salt stress. Finally, YvcA, a member of the transient receptor potential channel (TRPC) protein family of vacuolar Ca2+channels, was proven to compensate for calcineurin-CchA in fungal salt stress adaption.IMPORTANCEThe feedback inhibition relationship between calcineurin and the calcium channel Cch1/Mid1 has been well recognized from yeast. Interestingly, our previous study (S. Wang et al., PLoS One7:e46564, 2012,http://dx.doi.org/10.1371/journal.pone.0046564) showed that the deletion ofcchAcould suppress the hyphal growth defects caused by the loss of calcineurin under salt stress inAspergillus nidulans. In this study, our findings suggest that fungi are able to develop a unique mechanism for adapting to environmental salt stress. Compared to cells cultured normally, the NaCl-pretreated cells had a remarkable increase in transient [Ca2+]c. Furthermore, we show that calcineurin and CchA are required to modulate cellular calcium levels and synergistically coordinate calcium influx under salt stress. Finally, YvcA, a member of of the TRPC family of vacuolar Ca2+channels, was proven to compensate for calcineurin-CchA in fungal salt stress adaption. The findings in this study provide insights into the complex regulatory links between calcineurin and CchA to maintain cytoplasmic Ca2+homeostasis in response to different environments.

scholarly journals Functional Analysis of Sterol Transporter Orthologues in the Filamentous Fungus Aspergillus nidulans

2015 ◽  
Vol 14 (9) ◽  
pp. 908-921 ◽  
Author(s):  
Nicole Bühler ◽  
Daisuke Hagiwara ◽  
Norio Takeshita
Keyword(s):  
Plasma Membrane ◽  
Aspergillus Nidulans ◽  
Filamentous Fungi ◽  
Gene Deletion ◽  
Fluorescent Protein ◽  
Fungal Growth ◽  
Hyphal Growth ◽  
Apical Plasma Membrane ◽  
Important Species ◽  
Content Type

ABSTRACT Polarized growth in filamentous fungi needs a continuous supply of proteins and lipids to the growing hyphal tip. One of the important membrane compounds in fungi is ergosterol. At the apical plasma membrane ergosterol accumulations, which are called sterol-rich plasma membrane domains (SRDs). The exact roles and formation mechanism of the SRDs remained unclear, although the importance has been recognized for hyphal growth. Transport of ergosterol to hyphal tips is thought to be important for the organization of the SRDs. Oxysterol binding proteins, which are conserved from yeast to human, are involved in nonvesicular sterol transport. In Saccharomyces cerevisiae seven oxysterol-binding protein homologues (OSH1 to -7) play a role in ergosterol distribution between closely located membranes independent of vesicle transport. We found five homologous genes ( oshA to oshE ) in the filamentous fungi Aspergillus nidulans . The functions of OshA-E were characterized by gene deletion and subcellular localization. Each gene-deletion strain showed characteristic phenotypes and different sensitivities to ergosterol-associated drugs. Green fluorescent protein-tagged Osh proteins showed specific localization in the late Golgi compartments, puncta associated with the endoplasmic reticulum, or diffusely in the cytoplasm. The genes expression and regulation were investigated in a medically important species Aspergillus fumigatus , as well as A. nidulans . Our results suggest that each Osh protein plays a role in ergosterol distribution at distinct sites and contributes to proper fungal growth.

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