Molecular cloning of Rab-related genes in the yeast Yarrowia lipolytica. Analysis of RYL1, an essential gene encoding a SEC4 homologue

1995 ◽  
Vol 27 (2) ◽  
pp. 123-130 ◽  
Author(s):  
Brigitte Pertuiset ◽  
Jean-Marie Beckerich ◽  
Claude Gaillardin
Keyword(s):  
Molecular Cloning ◽  
Yarrowia Lipolytica ◽  
Essential Gene ◽  
Gene Encoding ◽  
Yeast Yarrowia Lipolytica

scholarly journals A Rac Homolog Is Required for Induction of Hyphal Growth in the Dimorphic Yeast Yarrowia lipolytica

2000 ◽  
Vol 182 (9) ◽  
pp. 2376-2386 ◽  
Author(s):  
Cleofe A. R. Hurtado ◽  
Jean-Marie Beckerich ◽  
Claude Gaillardin ◽  
Richard A. Rachubinski
Keyword(s):  
Yarrowia Lipolytica ◽  
Blot Analysis ◽  
Zinc Finger Protein ◽  
Essential Gene ◽  
Hyphal Growth ◽  
Fungal Species ◽  
Gene Encoding ◽  
Adverse Conditions ◽  
Acid Protein ◽  
Dimorphic Yeast

ABSTRACT Dimorphism in fungi is believed to constitute a mechanism of response to adverse conditions and represents an important attribute for the development of virulence by a number of pathogenic fungal species. We have isolated YlRAC1, a gene encoding a 192-amino-acid protein that is essential for hyphal growth in the dimorphic yeast Yarrowia lipolytica and which represents the first Rac homolog described for fungi. YlRAC1 is not an essential gene, and its deletion does not affect the ability to mate or impair actin polarization in Y. lipolytica. However, strains lacking functional YlRAC1 show alterations in cell morphology, suggesting that the function of YlRAC1 may be related to some aspect of the polarization of cell growth. Northern blot analysis showed that transcription of YlRAC1 increases steadily during the yeast-to-hypha transition, while Southern blot analysis of genomic DNA suggested the presence of severalRAC family members in Y. lipolytica. Interestingly, strains lacking functional YlRAC1 are still able to grow as the pseudohyphal form and to invade agar, thus pointing to a function for YlRAC1 downstream of MHY1, a previously isolated gene encoding a C2H2-type zinc finger protein with the ability to bind putative stress response elements and whose activity is essential for both hyphal and pseudohyphal growth in Y. lipolytica.

Effect of Copper on Acid Phosphatase Activity in Yeast Yarrowia lipolytica

2007 ◽  
Vol 62 (1-2) ◽  
pp. 70-76 ◽  
Author(s):  
Hiroyasu Ito ◽  
Masahiro Inouhe ◽  
Hiroshi Tohoyama ◽  
Masanori Joho
Keyword(s):  
Acid Phosphatase ◽  
Yarrowia Lipolytica ◽  
Acid Phosphatase Activity ◽  
Inorganic Phosphate ◽  
Soluble Form ◽  
Gene Encoding ◽  
Effect Of Copper ◽  
Yeast Yarrowia Lipolytica ◽  
Apase Activity

Acid phosphatase (APase) activity of the yeast Yarrowia lipolytica increased with increasing Cu2+ concentrations in the medium. Furthermore, the enzyme in soluble form was stimulated in vitro by Cu2+, Co2+, Ni2+, Mn2+ and Mg2+ and inhibited by Ag+ and Cd2+. The most effective ion was Cu2+, especially for the enzyme from cultures in medium containing Cu2+, whereas APase activity in wall-bound fragments was only slightly activated by Cu2+. The content of cellular phosphate involving polyphosphate was decreased by adding Cu2+, regardless of whether or not the medium was rich in inorganic phosphate. Overproduction of the enzyme stimulated by Cu2+ might depend on derepression of the gene encoding the APase isozyme.

Cloning of the gene encoding the catalytic subunit of casein kinase II from the yeast Yarrowia lipolytica

1997 ◽  
Vol 256 (4) ◽  
pp. 355-364 ◽  
Author(s):  
P. H. Benetti ◽  
S. I. Kim ◽  
M. Canonge ◽  
T. Chardot ◽  
J. C. Meunier
Keyword(s):  
Yarrowia Lipolytica ◽  
Casein Kinase Ii ◽  
Casein Kinase ◽  
Catalytic Subunit ◽  
Gene Encoding ◽  
Yeast Yarrowia Lipolytica

Molecular cloning of YlPMR1, a S. cerevisiae PMR1 homologue encoding a novel P-type secretory pathway Ca2+-ATPase, in the yeast Yarrowia lipolytica

Gene ◽  
1998 ◽  
Vol 206 (1) ◽  
pp. 107-116 ◽  
Author(s):  
Cheon Seok Park ◽  
Jeong-Yoon Kim ◽  
Caroline Crispino ◽  
Ching Chuan Chang ◽  
Dewey D.Y Ryu
Keyword(s):  
Molecular Cloning ◽  
Yarrowia Lipolytica ◽  
Secretory Pathway ◽  
P Type ◽  
Yeast Yarrowia Lipolytica

scholarly journals Engineering of the Yeast Yarrowia lipolytica for the Production of Glycoproteins Lacking the Outer-Chain Mannose Residues of N-Glycans

2007 ◽  
Vol 73 (14) ◽  
pp. 4446-4454 ◽  
Author(s):  
Yunkyoung Song ◽  
Min Hee Choi ◽  
Jeong-Nam Park ◽  
Moo Woong Kim ◽  
Eun Jung Kim ◽  
...  
Keyword(s):  
Yarrowia Lipolytica ◽  
Mutant Strain ◽  
Null Mutant ◽  
Wild Type ◽  
Core Oligosaccharide ◽  
Gene Encoding ◽  
The Core ◽  
Secretory Glycoproteins ◽  
Yeast Yarrowia Lipolytica

ABSTRACT In an attempt to engineer a Yarrowia lipolytica strain to produce glycoproteins lacking the outer-chain mannose residues of N-linked oligosaccharides, we investigated the functions of the OCH1 gene encoding a putative α-1,6-mannosyltransferase in Y. lipolytica. The complementation of the Saccharomyces cerevisiae och1 mutation by the expression of YlOCH1 and the lack of in vitro α-1,6-mannosyltransferase activity in the Yloch1 null mutant indicated that YlOCH1 is a functional ortholog of S. cerevisiae OCH1. The oligosaccharides assembled on two secretory glycoproteins, the Trichoderma reesei endoglucanase I and the endogenous Y. lipolytica lipase, from the Yloch1 null mutant contained a single predominant species, the core oligosaccharide Man8GlcNAc2, whereas those from the wild-type strain consisted of oligosaccharides with heterogeneous sizes, Man8GlcNAc2 to Man12GlcNAc2. Digestion with α-1,2- and α-1,6-mannosidase of the oligosaccharides from the wild-type and Yloch1 mutant strains strongly supported the possibility that the Yloch1 mutant strain has a defect in adding the first α-1,6-linked mannose to the core oligosaccharide. Taken together, these results indicate that YlOCH1 plays a key role in the outer-chain mannosylation of N-linked oligosaccharides in Y. lipolytica. Therefore, the Yloch1 mutant strain can be used as a host to produce glycoproteins lacking the outer-chain mannoses and further developed for the production of therapeutic glycoproteins containing human-compatible oligosaccharides.

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