Cloning of the isocitrate lyase gene (ICL1) from Yarrowia lipolytica and characterization of the deduced protein

1993 ◽  
Vol 241-241 (3-4) ◽  
pp. 422-430 ◽  
Author(s):  
Gerold Barth ◽  
Thomas Scheuber
Keyword(s):  
Yarrowia Lipolytica ◽  
Isocitrate Lyase

Characterization of major protein phosphatases from selected species of Kluyveromyces. Comparison with protein phosphatases from Yarrowia lipolytica

2001 ◽  
Vol 47 (9) ◽  
pp. 861-870 ◽  
Author(s):  
Pascale Jolivet ◽  
Edith Bergeron ◽  
Haguith Benyair ◽  
Jean-Claude Meunier
Keyword(s):  
Acid Phosphatase ◽  
Yarrowia Lipolytica ◽  
Protein Phosphatase ◽  
Protein Phosphatases ◽  
Major Protein ◽  
Ethanol Treatment ◽  
Early Stationary Phase ◽  
Yeast Strains ◽  
Deficient Medium

Casein phosphatase activities have been identified in five yeast strains grown on Pi-deficient medium. Maximal endocellular activities appeared in the exponential phase. Exocellular phosphatases were significantly produced from Yarrowia lipolytica W-29 and Kluyveromyces marxianus, in the early stationary phase. Major phosphatases from K. marxianus were one heavy acid phosphatase composed of 64–67 kDa subunits, which could be secreted in the medium, and one type 2A protein phosphatase with an apparent molecular mass of 147 kDa and a 52 kDa catalytic subunit dissociated by 80% ethanol treatment. The characteristics of phosphatases purified from K. marxianus were compared with those previously purified from Y. lipolytica.Key words: yeast, type 2A protein phosphatase, acid phosphatase, [32P]casein, Pi deficiency.

scholarly journals The Identification and Characterization of ADR6, a Gene Required for Sporulation and for Expression of the Alcohol Dehydrogenase II Isozyme From Saccharomyces cerevisiae

Genetics ◽  
1987 ◽  
Vol 116 (4) ◽  
pp. 523-530
Author(s):  
Aileen K W Taguchi ◽  
Elton T Young
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Alcohol Dehydrogenase ◽  
Isocitrate Lyase ◽  
Carbon Sources ◽  
Recessive Mutation ◽  
Yeast Saccharomyces Cerevisiae ◽  
Upstream Activating Sequence ◽  
Adh Activity ◽  
Identification And Characterization

ABSTRACT The alcohol dehydrogenase II isozyme (enzyme, ADHII; structural gene, ADH2) of the yeast, Saccharomyces cerevisiae, is under stringent carbon catabolite control. This cytoplasmic isozyme exhibits negligible activity during growth in media containing fermentable carbon sources such as glucose and is maximal during growth on nonfermentable carbon sources. A recessive mutation, adr6-1, and possibly two other alleles at this locus, were selected for their ability to decrease Ty-activated ADH2-6 c expression. The adr6-1 mutation led to decreased ADHII activity in both ADH2-6c and ADH2+ strains, and to decreased levels of ADH2 mRNA. Ty transcription and the expression of two other carbon catabolite regulated enzymes, isocitrate lyase and malate dehydrogenase, were unaffected by the adr6-1 mutation. adr6-1/adr6-1strains were defective for sporulation, indicating that adr6 mutations may have pleiotropic effects. The sporulation defect was not a consequence of decreased ADH activity. Since the ADH2-6c mutation is due to insertion of a 5.6-kb Ty element at the TATAA box, it appears that the ADR6+-dependent ADHII activity required ADH2 sequences 3′ to or including the TATAA box. The ADH2 upstream activating sequence (UAS) was probably not required. The ADR6 locus was unlinked to the ADR1 gene which encodes another trans-acting element required for ADH2 expression.

Purification and Characterization of Isocitrate Lyase from Ethanol-grown Euglena gracilis

1994 ◽  
Vol 41 (6) ◽  
pp. 536-539 ◽  
Author(s):  
KOUKI ONO ◽  
MASAHIRO OKIHASHI ◽  
HIROSHI INUI ◽  
KAZUTAKA MIYATAKE ◽  
SHOZABURO KITAOKA ◽  
...  
Keyword(s):  
Euglena Gracilis ◽  
Isocitrate Lyase ◽  
Purification And Characterization

Isolation and characterization of dominant mutations resistant to carbon catabolite repression of galactokinase synthesis in Saccharomyces cerevisiae

1981 ◽  
Vol 1 (2) ◽  
pp. 83-93
Author(s):  
K Matsumoto ◽  
A Toh-e ◽  
Y Oshima
Keyword(s):  
Partial Resistance ◽  
Carbon Catabolite Repression ◽  
Glucose Repression ◽  
Isocitrate Lyase ◽  
Isolation And Characterization ◽  
Enhanced Resistance ◽  
Leloir Pathway ◽  
Resistant Mutants ◽  
A Site

Seven dominant mutations showing greatly enhanced resistance to the glucose repression of galactokinase synthesis have been isolated from GAL81 mutants, which have the constitutive phenotype but are still strongly repressible by glucose for the synthesis of the Leloir enzymes. These glucose-resistant mutants were due to semidominant mutations at either of two loci, GAL82 and GAL83. Both loci are unlinked to the GAL81- gal4, gal80, or gal7 X gal10 X gal1 locus or to each other. The GAL83 locus was mapped on chromosome V at a site between arg9 and cho1. The GAL82 and GAL83 mutations produced partial resistance of galactokinase to glucose repression only when one or both of these mutations were combined with a GAL81 or a gal80 mutation. The GAL82 and GAL83 mutations are probably specific for expression of the Leloir pathway and related enzymes, because they do not affect the synthesis of alpha-D-glucosidase, invertase, or isocitrate lyase.

Construction and characterization of a Yarrowia lipolytica mutant lacking genes encoding cytochromes P450 subfamily 52

2012 ◽  
Vol 49 (1) ◽  
pp. 58-64 ◽  
Author(s):  
Hiroshi Takai ◽  
Ryo Iwama ◽  
Satoshi Kobayashi ◽  
Hiroyuki Horiuchi ◽  
Ryouichi Fukuda ◽  
...  
Keyword(s):  
Yarrowia Lipolytica ◽  
Cytochromes P450 ◽  
Genes Encoding

scholarly journals Characterization of a bioemulsifier produced from glycerol and glucose by Yarrowia lipolytica

2009 ◽  
Vol 25 ◽  
pp. S138 ◽  
Author(s):  
P. Amaral ◽  
M. Colão ◽  
M.A. Coelho ◽  
G. Fontes ◽  
M. Nele
Keyword(s):  
Yarrowia Lipolytica

Characterization of a nontoxic pyomelanin pigment produced by the yeast Yarrowia lipolytica

2020 ◽  
Vol 36 (2) ◽  
Author(s):  
Imen Ben Tahar ◽  
Małgorzata Kus‐Liśkiewicz ◽  
Yannick Lara ◽  
Emmanuelle Javaux ◽  
Patrick Fickers
Keyword(s):  
Yarrowia Lipolytica ◽  
Yeast Yarrowia Lipolytica

scholarly journals The Gluconeogenic Enzyme Fructose-1,6-Bisphosphatase Is Dispensable for Growth of the Yeast Yarrowia lipolytica in Gluconeogenic Substrates

2008 ◽  
Vol 7 (10) ◽  
pp. 1742-1749 ◽  
Author(s):  
Raquel Jardón ◽  
Carlos Gancedo ◽  
Carmen-Lisset Flores
Keyword(s):  
Yarrowia Lipolytica ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Isocitrate Lyase ◽  
Carbon Sources ◽  
Subcellular Fractionation ◽  
Fructose 1,6 Bisphosphatase ◽  
Genes Encoding ◽  
Key Enzyme ◽  
Gluconeogenic Enzyme ◽  
Fructose 1,6 Bisphosphate

ABSTRACT The genes encoding gluconeogenic enzymes in the nonconventional yeast Yarrowia lipolytica were found to be differentially regulated. The expression of Y. lipolytica FBP1 (YlFBP1) encoding the key enzyme fructose-1,6-bisphosphatase was not repressed by glucose in contrast with the situation in other yeasts; however, this sugar markedly repressed the expression of YlPCK1, encoding phosphoenolpyruvate carboxykinase, and YlICL1, encoding isocitrate lyase. We constructed Y. lipolytica strains with two different disrupted versions of YlFBP1 and found that they grew much slower than the wild type in gluconeogenic carbon sources but that growth was not abolished as happens in most microorganisms. We attribute this growth to the existence of an alternative phosphatase with a high Km (2.3 mM) for fructose-1,6-bisphosphate. The gene YlFBP1 restored fructose-1,6-bisphosphatase activity and growth in gluconeogenic carbon sources to a Saccharomyces cerevisiae fbp1 mutant, but the introduction of the FBP1 gene from S. cerevisiae in the Ylfbp1 mutant did not produce fructose-1,6-bisphosphatase activity or growth complementation. Subcellular fractionation revealed the presence of fructose-1,6-bisphosphatase both in the cytoplasm and in the nucleus.

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