The extracellular acid protease gene of Yarrowia lipolytica: sequence and pH-regulated transcription

Young, Thomas W.; Wadeson, Albert; Glover, David; Quincey, R. V.; Butlin, Michael J.; Kamei, Elizabeth A.

doi:10.1099/13500872-142-10-2913

Cited by 34 publications

(35 citation statements)

References 26 publications

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“…Although a signal peptide was detected for the DNA-deduced Axp aspartic protease of Y. lipolytica 148, the prepro region of the protein shared no homology with other extracellular proteins, and the secretory motif of the protein was distinct from the common motif for yeast extracellular protease processing (54). McEwen and Young (32) could not confirm whether the Axp precursor contains the signal peptide, but it was confirmed that Axp translocation occurs cotranslationally.…”

Section: Discussionmentioning

confidence: 78%

Identification and Partial Characterization of Extracellular Aspartic Protease Genes from Metschnikowia pulcherrima IWBT Y1123 and Candida apicola IWBT Y1384

Reid

Theron

Toit

et al. 2012

Appl Environ Microbiol

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ABSTRACTThe extracellular acid proteases of non-Saccharomyceswine yeasts may fulfill a number of roles in winemaking, which include increasing the available nitrogen sources for the growth of fermentative microbes, affecting the aroma profile of the wine, and potentially reducing protein haze formation. These proteases, however, remain poorly characterized, especially at genetic level. In this study, two extracellular aspartic protease-encoding genes were identified and sequenced, from two yeast species of enological origin: one gene fromMetschnikowia pulcherrimaIWBT Y1123, namedMpAPr1, and the other gene fromCandida apicolaIWBT Y1384, namedCaAPr1.In silicoanalysis of these two genes revealed a number of features peculiar to aspartic protease genes, and both the MpAPr1 and CaAPr1 putative proteins showed homology to proteases of yeast genera. Heterologous expression ofMpAPr1inSaccharomyces cerevisiaeYHUM272 confirmed that it encodes an aspartic protease. MpAPr1 production, which was shown to be constitutive, and secretion were confirmed in the presence of bovine serum albumin (BSA), casein, and grape juice proteins. TheMpAPr1gene was found to be present in 12 otherM. pulcherrimastrains; however, plate assays revealed that the intensity of protease activity was strain dependent and unrelated to the gene sequence.

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Section: Discussionmentioning

confidence: 78%

Identification and Partial Characterization of Extracellular Aspartic Protease Genes from Metschnikowia pulcherrima IWBT Y1123 and Candida apicola IWBT Y1384

Reid

Theron

Toit

et al. 2012

Appl Environ Microbiol

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“…The 5Ј upstream region of the AXP gene expressed at acidic pH (53) carries no copy of the full decameric sequence but three copies of the core PacC hexanucleotide (Table 3). The significance of these sites is unclear, since a repressing effect of the truncated YlRim101p forms could be evidenced only at …”

Section: Discussionmentioning

confidence: 99%

Genetic Analysis of Regulatory Mutants Affecting Synthesis of Extracellular Proteinases in the Yeast Yarrowia lipolytica: Identification of a RIM101/pacC Homolog

Lambert

Blanchin‐Roland

Louedec

et al. 1997

Molecular and Cellular Biology

107

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Depending on the pH of the growth medium, the yeast Yarrowia lipolytica secretes both an acidic proteinase and an alkaline proteinase, the synthesis of which is also controlled by carbon, nitrogen, and sulfur availability, as well as by the presence of extracellular proteins. Recessive mutations at four unlinked loci, named PAL1 to PAL4, were isolated which prevent alkaline proteinase derepression under conditions of carbon and nitrogen limitation at pH 6.8. These mutations markedly affect mating and sporulation. A dominant suppressor of all four PAL mutations was isolated from a wild-type genomic library, which turned out to be a C-terminally truncated form of a 585-residue transcriptional factor of the His 2 Cys 2 zinc finger family, which we propose to call YlRim101p. Another C-terminally truncated version of YlRim101p (419 residues) is encoded by the dominant RPH2 mutation previously isolated as expressing alkaline protease independently of the pH. YlRim101p is homologous to the transcriptional activators Rim101p of Saccharomyces cerevisiae, required for entry into meiosis, and PacC of Aspergillus nidulans and Penicillium chrysogenum, which were recently shown to mediate regulation by ambient pH. YlRim101p appears essential for mating and sporulation and for alkaline proteinase derepression. YlRIM101 expression is autoregulated, maximal at alkaline pH, and strongly impaired by PAL mutations.

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“…Moreover, protease production is tightly controlled by a combination of environmental stimuli, which includes nutrient availability such as carbon, nitrogen, and sulfur starvation (Gonzalez-Lopez et al, 2002). The presence of nitrogen (ammonium ions, amino acids) and sulfur can have a repressive effect on AEP and AXP production (Young et al, 1996).…”

Section: Effect Of Nitrogen Source On Lipase Productionmentioning

confidence: 99%

NITROGEN SOURCES ON TPOMW VALORIZATION THROUGH SOLID STATE FERMENTATION PERFORMED BY Yarrowia lipolytica

Lopes

Farias

Belo

et al. 2016

Braz. J. Chem. Eng.

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-This manuscript reports the valorization of two-phase olive mill waste (TPOMW) as raw material and carbon source for solid state fermentation using Yarrowia lipolytica as biocatalyst. Due to its chemical characteristics, a combination of different raw materials (TPOMW and wheat bran, WB) was evaluated and two distinct nitrogen sources were applied as supplementation for lipase production. A TPOMW/WB ratio of 1:1 and supplementation with ammonium sulfate was chosen as the best condition. The productivity in 24 h reached 7.8 U/g*h and, after four days of process, only decreased about 35%. Process pH ranged from 5.5 -5.9, remaining in an acid range. Thus, the successful use of TPOMW, a watery solid by-product with high content of lipids, as raw material for Yarrowia lipolytica growth and lipase production provided an environmental friendly alternative to valorize such waste.

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The extracellular acid protease gene of Yarrowia lipolytica: sequence and pH-regulated transcription

Cited by 34 publications

References 26 publications

Identification and Partial Characterization of Extracellular Aspartic Protease Genes from Metschnikowia pulcherrima IWBT Y1123 and Candida apicola IWBT Y1384

Identification and Partial Characterization of Extracellular Aspartic Protease Genes from Metschnikowia pulcherrima IWBT Y1123 and Candida apicola IWBT Y1384

Genetic Analysis of Regulatory Mutants Affecting Synthesis of Extracellular Proteinases in the Yeast Yarrowia lipolytica: Identification of a RIM101/pacC Homolog

NITROGEN SOURCES ON TPOMW VALORIZATION THROUGH SOLID STATE FERMENTATION PERFORMED BY Yarrowia lipolytica

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