Aspergillus nidulans hypB encodes a Sec7-domain protein important for hyphal morphogenesis

2008 ◽  
Vol 45 (5) ◽  
pp. 749-759 ◽  
Author(s):  
Yi Yang ◽  
Amira M. El-Ganiny ◽  
Geoffrey E. Bray ◽  
David A.R. Sanders ◽  
Susan G.W. Kaminskyj
PLoS ONE ◽  
2015 ◽  
Vol 10 (9) ◽  
pp. e0137554 ◽  
Author(s):  
Fahad Alkahyyat ◽  
Min Ni ◽  
Sun Chang Kim ◽  
Jae-Hyuk Yu

2001 ◽  
Vol 39 (1) ◽  
pp. 25-34 ◽  
Author(s):  
Effie Kosmidou ◽  
Patricia Lunness ◽  
John H. Doonan

2004 ◽  
Vol 82 (6) ◽  
pp. 807-814 ◽  
Author(s):  
Susan GW Kaminskyj ◽  
Melissa R Boire

Aspergillus nidulans Eidam (G. Wint.) wild-type hyphal morphogenesis requires the hypA gene product. Like its homolog in Saccharomyces cerevisiae Meyen ex E.C. Hansen, TRS120, hypA encodes a cytoplasmic protein likely associated with endomem branes. hypA is not essential, but hypA1 temperature-sensitive strains grow poorly at restrictive temperatures. In younger cells, endomembrane arrays were aberrant, only sometimes resembling wild type. In older cells, Golgi equivalents were swollen, impacted with electron-dense granules. In hypA1 strains grown at 42 °C, the poorly polarized hyphae lack recognizable Spitzenkörper and have walls at least four-fold thicker than those of wild-type or hypA1 strains grown at 28 °C. At restrictive temperatures, both hyphal width and wall thickness increase markedly in basal regions, suggesting wall deposition is impaired. Septa are thicker than in wild type, but have medial pores and Woronin bodies. Individual nuclei and mitochondria are smaller at 42 °C than at 28 °C, but each collectively occupies similar proportions of the cytoplasm. Mitochondrial cristae are reduced in number and width at 42 °C, possibly compromising metabolic efficiency; in older cells, cristae are widely spaced and randomly inserted. If hypA1 cells grown at 42 °C are shifted to 28 °C, the thickened wall is precisely degraded for growth of wild-type branches, which form within 1 h, suggesting areas of nascent polarity formed at 42 °C require the hypA product for wild-type function.Key words: endomembrane, filamentous fungus, electron microscopy, cell wall, secretion, Saccharomyces TRS120.


2006 ◽  
Vol 17 (3) ◽  
pp. 1218-1227 ◽  
Author(s):  
Shaojie Li ◽  
Liangcheng Du ◽  
Gary Yuen ◽  
Steven D. Harris

In filamentous fungi, the stabilization of a polarity axis is likely to be a pivotal event underlying the emergence of a germ tube from a germinating spore. Recent results implicate the polarisome in this process and also suggest that it requires localized membrane organization. Here, we employ a chemical genetic approach to demonstrate that ceramide synthesis is necessary for the formation of a stable polarity axis in the model fungus Aspergillus nidulans. We demonstrate that a novel compound (HSAF) produced by a bacterial biocontrol agent disrupts polarized growth and leads to loss of membrane organization and formin localization at hyphal tips. We show that BarA, a putative acyl-CoA-dependent ceramide synthase that is unique to filamentous fungi mediates the effects of HSAF. Moreover, A. nidulans possesses a second likely ceramide synthase that is essential and also regulates hyphal morphogenesis. Our results suggest that filamentous fungi possess distinct pools of ceramide that make independent contributions to polarized hyphal growth, perhaps through the formation of specialized lipid microdomains that regulate organization of the cytoskeleton.


2007 ◽  
Vol 0 (0) ◽  
pp. 071115150640001-??? ◽  
Author(s):  
Aleksandra Virag ◽  
Maurice P. Lee ◽  
Haoyu Si ◽  
Steven D. Harris

1999 ◽  
Vol 3 (3) ◽  
pp. 275-285 ◽  
Author(s):  
Anne Peyroche ◽  
Bruno Antonny ◽  
Sylviane Robineau ◽  
Joel Acker ◽  
Jacqueline Cherfils ◽  
...  

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