scholarly journals Oxidation of methanol by the yeast Pichia pastoris. Purification and properties of the formate dehydrogenase.

1983 ◽  
Vol 47 (11) ◽  
pp. 2547-2554 ◽  
Author(s):  
J. J. ALLAIS ◽  
A. LOUKTIBI ◽  
J. BARATTI
Keyword(s):  
Pichia Pastoris ◽  
Formate Dehydrogenase ◽  
Yeast Pichia Pastoris ◽  
Oxidation Of Methanol ◽  
Purification And Properties

Isolation of alcohol oxidase and two other methanol regulatable genes from the yeast Pichia pastoris

1985 ◽  
Vol 5 (5) ◽  
pp. 1111-1121
Author(s):  
S B Ellis ◽  
P F Brust ◽  
P J Koutz ◽  
A F Waters ◽  
M M Harpold ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Carbon Source ◽  
Sole Carbon Source ◽  
Alcohol Oxidase ◽  
Methylotrophic Yeasts ◽  
Sequence Analyses ◽  
Yeast Pichia Pastoris ◽  
Oxidation Of Methanol ◽  
Regulated Expression

The oxidation of methanol follows a well-defined pathway and is similar for several methylotrophic yeasts. The use of methanol as the sole carbon source for the growth of Pichia pastoris stimulates the expression of a family of genes. Three methanol-responsive genes have been isolated; cDNA copies have been made from mRNAs of these genes, and the protein products from in vitro translations have been examined. The identification of alcohol oxidase as one of the cloned, methanol-regulated genes has been made by enzymatic, immunological, and sequence analyses. Methanol-regulated expression of each of these three isolated genes can be demonstrated to occur at the level of transcription. Finally, DNA subfragments of two of the methanol-responsive genomic clones from P. pastoris have been isolated and tentatively identified as containing the control regions involved in methanol regulation.

Divergent modes of autophagy in the methylotrophic yeast Pichia pastoris

1995 ◽  
Vol 108 (1) ◽  
pp. 25-35 ◽  
Author(s):  
D.L. Tuttle ◽  
W.A. Dunn
Keyword(s):  
Protein Synthesis ◽  
Pichia Pastoris ◽  
Carbon Source ◽  
Formate Dehydrogenase ◽  
Alcohol Oxidase ◽  
Methylotrophic Yeast ◽  
Intermediate Stage ◽  
Peroxisomal Enzyme ◽  
Yeast Pichia Pastoris ◽  
Methylotrophic Yeast Pichia Pastoris

The budding yeast Pichia pastoris responds to methanolic media by synthesizing high levels of cytosolic enzymes (e.g. formate dehydrogenase) and peroxisomal enzymes (e.g. alcohol oxidase), which are necessary to assimilate this carbon source. Major alterations in cellular metabolism are initiated upon a shift in carbon source to ethanol or glucose. These alterations require the synthesis of new proteins and the rapid degradation of those enzymes no longer needed for methanol utilization. In this study, we have measured cytosolic and peroxisomal enzyme activities and examined the fate of morphologically distinct peroxisomes to assess the degradative response of this yeast during nutrient adaptation. Utilizing biochemical, morphological and genetic approaches, we have shown that there exist in P. pastoris at least two pathways for the sequestration of peroxisomes into the vacuole for degradation. The ethanol-induced pathway is independent of protein synthesis and includes an intermediate stage in which individual peroxisomes are sequestered into autophagosomes by wrapping membranes, which then fuse with the vacuole. This process is analogous to macroautophagy. The glucose-induced pathway invokes the engulfment of clusters of peroxisomes by finger-like protrusions of the vacuole by a process analogous to microautophagy. Unlike ethanol adaptation, glucose stimulated the degradation of formate dehydrogenase as well. Peroxisomes remained outside the vacuoles of glucose-adapted cycloheximide-treated normal cells, suggesting that protein synthesis is required for peroxisome entry into the yeast vacuole. Two complementary mutants (gsa1 and gsa2) that are unable to degrade peroxisomes or formate dehydrogenase during glucose adaptation were isolated. The mutated gene products appear to function in one or more events upstream of degradation within the vacuole, since ethanol-induced peroxisome degradation proceeded normally in these mutants and peroxisomes were found outside the vacuoles of glucose-adapted gsa2 cells. Mutants lacking vacuolar proteinases A and B were unable to degrade alcohol oxidase or formate dehydrogenase during ethanol or glucose adaptation. Peroxisomes were found to accumulate within the vacuoles of these proteinase mutants during adaptation. Combined, the results suggest that there exist in Pichia pastoris two independent pathways for the sequestration of peroxisomes into the vacuole, the site of degradation.

scholarly journals Isolation of alcohol oxidase and two other methanol regulatable genes from the yeast Pichia pastoris.

1985 ◽  
Vol 5 (5) ◽  
pp. 1111-1121 ◽  
Author(s):  
S B Ellis ◽  
P F Brust ◽  
P J Koutz ◽  
A F Waters ◽  
M M Harpold ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Carbon Source ◽  
Sole Carbon Source ◽  
Alcohol Oxidase ◽  
Methylotrophic Yeasts ◽  
Sequence Analyses ◽  
Yeast Pichia Pastoris ◽  
Oxidation Of Methanol ◽  
Regulated Expression

The oxidation of methanol follows a well-defined pathway and is similar for several methylotrophic yeasts. The use of methanol as the sole carbon source for the growth of Pichia pastoris stimulates the expression of a family of genes. Three methanol-responsive genes have been isolated; cDNA copies have been made from mRNAs of these genes, and the protein products from in vitro translations have been examined. The identification of alcohol oxidase as one of the cloned, methanol-regulated genes has been made by enzymatic, immunological, and sequence analyses. Methanol-regulated expression of each of these three isolated genes can be demonstrated to occur at the level of transcription. Finally, DNA subfragments of two of the methanol-responsive genomic clones from P. pastoris have been isolated and tentatively identified as containing the control regions involved in methanol regulation.

scholarly journals Adsorption process and mechanism of heavy metal ions by different components of cells, using yeast (Pichia pastoris) and Cu2+ as biosorption models

RSC Advances ◽  
2021 ◽  
Vol 11 (28) ◽  
pp. 17080-17091
Author(s):  
Xinggang Chen ◽  
Zhuang Tian ◽  
Haina Cheng ◽  
Gang Xu ◽  
Hongbo Zhou
Keyword(s):  
Heavy Metal ◽  
Pichia Pastoris ◽  
Metal Ions ◽  
Cell Walls ◽  
Heavy Metal Ions ◽  
Adsorption Process ◽  
Yeast Pichia Pastoris ◽  
Adsorption Sites

The Cu2+ first bound to the outer mannan and finally entered the cytoplasm. During the whole adsorption process, the number of adsorption sites in the outer and middle cell walls was the largest, and then gradually decreased.

The lipidome and proteome of microsomes from the methylotrophic yeast Pichia pastoris

2014 ◽  
Vol 1841 (2) ◽  
pp. 215-226 ◽  
Author(s):  
Lisa Klug ◽  
Pablo Tarazona ◽  
Clemens Gruber ◽  
Karlheinz Grillitsch ◽  
Brigitte Gasser ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Methylotrophic Yeast ◽  
Yeast Pichia Pastoris ◽  
Methylotrophic Yeast Pichia Pastoris
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