scholarly journals Accumulation of cellobiose lipids under nitrogen-limiting conditions by two ustilaginomycetous yeasts,Pseudozyma aphidisandPseudozyma hubeiensis

2013 ◽  
Vol 13 (1) ◽  
pp. 44-49 ◽  
Author(s):  
Tomotake Morita ◽  
Tokuma Fukuoka ◽  
Tomohiro Imura ◽  
Dai Kitamoto
Keyword(s):  
2014 ◽  
Vol 63 (7) ◽  
pp. 701-707 ◽  
Author(s):  
Ekaterina Kulakovskaya ◽  
Boris Baskunov ◽  
Anton Zvonarev
Keyword(s):  

2010 ◽  
Vol 77 (3) ◽  
pp. 926-933 ◽  
Author(s):  
Walid Hammami ◽  
Candy Quiroga Castro ◽  
Wilfried Rémus-Borel ◽  
Caroline Labbé ◽  
Richard R. Bélanger

ABSTRACTIn this work, we sought to understand how glycolipid production and the availability of nutrients could explain the ecology ofPseudozyma flocculosaand its biocontrol activity. For this purpose, we compared the development ofP. flocculosato that of a close relative, the plant pathogenUstilago maydis, under different environmental conditions. This approach was further supported by measuring the expression ofcyp1, a pivotal gene in the synthesis of unique antifungal cellobiose lipids of both fungi. On healthy cucumber and tomato plants, the expression ofcyp1remained unchanged over time inP. flocculosaand was undetected inU. maydis. At the same time, green fluorescent protein (GFP) strains of both fungi showed only limited green fluorescence on control leaves. On powdery mildew-infected cucumber leaves,P. flocculosainduced a complete collapse of the pathogen colonies, but glycolipid production, as studied bycyp1expression, was still comparable to that of controls. In complete contrast,cyp1was upregulated nine times whenP. flocculosawas applied toBotrytis cinerea-infected leaves, but the biocontrol fungus did not develop very well on the pathogen. Analysis of the possible nutrients that could stimulate the growth ofP. flocculosaon powdery mildew structures revealed that the complex Zn/Mn played a key role in the interaction. Other related fungi such asU. maydisdo not appear to have the same nutritional requirements and hence lack the ability to colonize powdery mildews. Whether production of antifungal glycolipids contributes to the release of nutrients from powdery mildew colonies is unclear, but the specificity of the biocontrol activity ofP. flocculosatoward Erysiphales does appear to be more complex than simple antibiosis.


2011 ◽  
Vol 77 (21) ◽  
pp. 7823-7829 ◽  
Author(s):  
Beate Teichmann ◽  
François Lefebvre ◽  
Caroline Labbé ◽  
Michael Bölker ◽  
Uwe Linne ◽  
...  

ABSTRACTFlocculosin and ustilagic acid (UA), two highly similar antifungal cellobiose lipids, are respectively produced byPseudozyma flocculosa, a biocontrol agent, andUstilago maydis, a plant pathogen. Both glycolipids contain a short-chain fatty acid hydroxylated at the β position but differ in the long fatty acid, which is hydroxylated at the α position in UA and at the β position in flocculosin. In both organisms, the biosynthesis genes are arranged in large clusters. The functions of most genes have already been characterized, but those of theP. flocculosa fhd1gene and its homolog fromU. maydis,uhd1, have remained undefined. The deduced amino acid sequences of these genes show homology to those of short-chain dehydrogenases and reductases (SDR). We disrupted theuhd1gene inU. maydisand analyzed the secreted UA.uhd1deletion strains produced UA lacking the β-hydroxyl group of the short-chain fatty acid. To analyze the function ofP. flocculosaFhd1, the corresponding gene was used to complementU. maydisΔuhd1mutants. Fhd1 was able to restore wild-type UA production, indicating that Fhd1 is responsible for β hydroxylation of the flocculosin short-chain fatty acid. We also investigated aP. flocculosahomolog of theU. maydislong-chain fatty-acid alpha hydroxylase Ahd1. TheP. flocculosa ahd1gene, which does not reside in the flocculosin gene cluster, was introduced intoU. maydisΔahd1mutant strains.P. flocculosaAhd1 neither complemented theU. maydisΔahd1phenotype nor resulted in the production of β-hydroxylated UA. This suggests thatP. flocculosaAhd1 is not involved in flocculosin hydroxylation.


2012 ◽  
Vol 61 (11) ◽  
pp. 659-664 ◽  
Author(s):  
Tomohiro Imura ◽  
Daisuke Kawamura ◽  
Yuko Ishibashi ◽  
Tomotake Morita ◽  
Shun Sato ◽  
...  

2005 ◽  
Vol 71 (6) ◽  
pp. 3033-3040 ◽  
Author(s):  
Sandra Hewald ◽  
Katharina Josephs ◽  
Michael Bölker

ABSTRACT The dimorphic basidiomycete Ustilago maydis produces large amounts of surface-active compounds under conditions of nitrogen starvation. These biosurfactants consist of derivatives of two classes of amphipathic glycolipids. Ustilagic acids are cellobiose lipids in which the disaccharide is O-glycosidically linked to 15,16-dihydroxyhexadecanoic acid. Ustilipids are mannosylerythritol lipids derived from acylated β-d-mannopyranosyl-d-erythritol. Whereas the chemical structure of these biosurfactants has been determined, the genetic basis for their biosynthesis and regulation is largely unknown. Here we report the first identification of two genes, emt1 and cyp1, that are essential for the production of fungal extracellular glycolipids. emt1 is required for mannosylerythritol lipid production and codes for a protein with similarity to prokaryotic glycosyltransferases involved in the biosynthesis of macrolide antibiotics. We suggest that Emt1 catalyzes the synthesis of mannosyl-d-erythritol by transfer of GDP-mannose. Deletion of the gene cyp1 resulted in complete loss of ustilagic acid production. Cyp1 encodes a cytochrome P450 monooxygenase which is highly related to a family of plant fatty acid hydroxylases. Therefore we assume that Cyp1 is directly involved in the biosynthesis of the unusual 15,16-dihydroxyhexadecanoic acid. We could show that mannosylerythritol lipid production is responsible for hemolytic activity on blood agar, whereas ustilagic acid secretion is required for long-range pheromone recognition. The mutants described here allow for the first time a genetic analysis of glycolipid production in fungi.


2011 ◽  
Vol 75 (8) ◽  
pp. 1597-1599 ◽  
Author(s):  
Tomotake MORITA ◽  
Yuko ISHIBASHI ◽  
Tokuma FUKUOKA ◽  
Tomohiro IMURA ◽  
Hideki SAKAI ◽  
...  

2009 ◽  
Vol 169 (2) ◽  
pp. 117-123 ◽  
Author(s):  
T. V. Kulakovskaya ◽  
W. I. Golubev ◽  
M. A. Tomashevskaya ◽  
E. V. Kulakovskaya ◽  
A. S. Shashkov ◽  
...  
Keyword(s):  

2014 ◽  
Vol 63 (10) ◽  
pp. 1005-1010 ◽  
Author(s):  
Tomohiro Imura ◽  
Shuhei Yamamoto ◽  
Chikako Yamashita ◽  
Toshiaki Taira ◽  
Hiroyuki Minamikawa ◽  
...  

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