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  • AERODYNAMICS
  • Analytical Chemistry and Spectroscopy
  • Animals
  • Life and Medical Sciences
  • Physics
  • Yeast
  • Springer  (6)
  • 1990-1994
  • 1975-1979  (6)
  • 1925-1929
  • 1979  (6)
Collection
Keywords
Publisher
Years
  • 1990-1994
  • 1975-1979  (6)
  • 1925-1929
Year
  • 1
    Electronic Resource
    Electronic Resource
    Recombination of yeast mitochondrial DNA does not require mitochondrial protein synthesis (1979)
    Springer
    Current genetics 1 (1979), S. 21-31 
    Details
    ISSN: 1432-0983
    Keywords: Yeast ; Mitochondrial DNA ; Recombination
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Mitochondrial genes recombine extensively in yeast zygotes. In heteropolar crosses (ω+ × ω−) in which the ω− “allele” consists of an insertion, there is preferential recovery of ω+ and markers closely linked to it. This polarity has been postulated to be a consequence of one-way gene conversion beginning at the ω locus (ω- to ω+). We have shown that most or all mitochondrial recombination in homopolar and heteropolar crosses, and the phenomenon of polarity itself, does not require products of protein synthesis on mitochondrial ribosomes. (i) Yeast strains were grown and mated, and the zygotes plated and grown, on glucose medium with erythromycin to inhibit and dilute out the products of mitochondrial protein synthesis. Recombination frequencies and polarity at the cap1 and oli1 loci were normal compared to controls in some homopolar (ω+ × ω−) and heteropolar crosses. Apparent changes in recombination frequencies and polarity were seen in other crosses but are attributable to locus-specific petite induction by erythromycin. (ii) Homopolar (ω+ × ω+) and heteropolar crosses between pairs of petite mutants retaining the cap1, ery1, and oli1 loci also showed nearly normal recombination at the cap1 and oli1 loci, as determined by test-crossing the petite progeny. The petite mutants and zygotes cannot do mitochondria) protein synthesis. These results support the recombinational model of polarity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00413304
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  • 2
    Electronic Resource
    Electronic Resource
    Sequestration of arginine by polyphosphate in vacuoles of yeast (Saccharomyces cerevisiae) (1979)
    Springer
    Archives of microbiology 121 (1979), S. 169-175 
    Details
    ISSN: 1432-072X
    Keywords: Yeast ; Vacuoles ; Compartmentation ; Polyphosphate ; Arginine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Isolated and purified vacuoles from yeast protoplasts contain the bulk of the cellular pool of arginine. The arginine is firmly retained in the isolated vacuoles despite of the presence of a permease which mediates arginine diffusion through the vacuolar membrane (Boller et al., 1975). It is shown, mainly by equilibrium dialysis, on vacuolar extracts, that the retention of arginine in the vacuoles is due to binding by polyphosphate. The polyphosphate appears to be located exclusively in the vacuoles. Enzymes hydrolysing polyphosphate are also located in the vacuoles. Isolated vacuoles from arginine grown cells contain about three times as much polyphosphate as vacuoles from ammonium grown cells; the vacuolar pool of arginine is correspondingly greater. Thus there seems to be a close correlation between the storage of arginine and polyphosphate. This confirms the observation that under conditions provoking “polyphosphate overcompensation” (Liss and Langen, 1962) the accumulation of enormous quantities of polyphosphate is associated with that of corresponding quantities of arginine, provided this amino acid is supplied in the medium. Yet, under certain growth conditions the cells are able to store, and to mobilize, both arginine and polyphosphate independently.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00689982
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  • 3
    Electronic Resource
    Electronic Resource
    Vacuoles: The sole compartments of digestive enzymes in yeast (Saccharomyces cerevisiae)? (1979)
    Springer
    Archives of microbiology 123 (1979), S. 23-35 
    Details
    ISSN: 1432-072X
    Keywords: Yeast ; Compartmentation ; Vacuoles ; Lysosome ; Cytosol ; ATPase ; Phosphatases ; Proteases ; Polyphosphate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Almost all the vacuoles (about 95%) remained intact after “polybase-induced lysis” of the yeast protoplasts. These vacuoles could be sedimentated together with other cell organelles which were equally well preserved, leaving as a supernatant a cytosol fraction which was essentially uncontaminated by the contents of disrupted vacuoles. After density gradient centrifugation more than half of the vacuoles were recovered in a fraction which was highly purified as judged from the measurement of several marker enzymes and from light and electron microscopic observations. Polyphosphate, which has been shown to be located exclusively in the vacuolar sap of protoplasts, was used as a vacuolar marker to determine the yields of vacuoles in the different fractions obtained from the density gradients. It was also used to assess the overall distribution of lytic enzymes in the cytosol and in the vacuome. The results indicate that the following enzyme activities are mostly, if not exclusively (〉90%), located in the vacuome, probably all in the typical large vacuoles present in the protoplasts: exo-and endopolyphosphatase, proteases A and B, carboxypeptidase Y, an aminopeptidase, RNase, α-mannosidase, and phosphatases which hydrolyze a number of different substrates. The polyphosphatases are thus in the same compartment as the polyphosphate. The activities of some other hydrolases, notably of a Mg2+ dependent, Oligomycin and NaN3 insensitive ATPase and alkaline phosphatase, were partially associated with the vacuoles. The activities of pyrophosphatase, tripolyphosphatase, α-glucosidase, and aminopeptidase active in the presence of EDTA, were located almost exclusively in the soluble, cytosolic fraction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00403499
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  • 4
    Electronic Resource
    Electronic Resource
    Pyruvate holo- and apocarboxylase content of biotin-deficient baker's yeast and the characteristics of the holoenzyme formation in permeabilized cells (1979)
    Springer
    Archives of microbiology 122 (1979), S. 121-127 
    Details
    ISSN: 1432-072X
    Keywords: Yeast ; Baker's yeast ; Biotin ; Biotinyl enzymes ; Pyruvate carboxylase ; Acetyl-CoA carboxylase ; Ureaamidolyase ; Pyruvate apocarboxylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The holo- and apocarboxylase proteins in baker's yeast grown in a chemostat at different biotin concentrations (from 0.1–200 μg/l) and on different carbon sources were assayed. The growth and the type of metabolism are considered with respect to the activity of the enzymes involved in oxaloacetate regeneration (pyruvate carboxylase and isocitrate lyase activities). In order to assay the level of apocarboxylase protein in the cells the characteristics of the pyruvate holocarboxylase formation in permeabilized cells were studied and thereby an assay method was developed. The pyruvate carboxylase activity of the cells grown in a medium with 4% glucose as the carbon source was almost constant from the lowest biotin concentration up to a biotin concentration of 10 μg/l, after which it rose and obtained a maximum at a biotin concentration of about 50 μg/l. The content of the apocarboxylase protein was maximal at 0.5 μg/l biotin, and then exceeded the level of the active pyruvate carboxylase protein by a factor of about 2.5. With increasing biotin concentration in the medium the content of apocarboxylase protein decreased and was negligible in cells grown at biotin concentrations higher than 100 μg/l. The total content of pyruvate carboxylase protein (i.e. apo- + holoenzyme) was roughly constant over a wide biotin concentration range (from 0.5–15 μg/l), the maximum being only double the minimum. At a biotin concentration 50 μg/l, where the maximum yield was reached, the cells still contained pyruvate apocarboxylase. The rapid increase in yield found around a biotin concentration of 10 μg/l correlates, on the basis of measured enzyme activities, more with the appearance of activity of glyoxylate cycle enzymes than with the increase in the activity of pyruvate carboxylase. When cells were growing on ethanol with biotin as the growth limiting factor, the cells still used biotin for the formation of pyruvate holocarboxylase, and proportionally more of the total content of pyruvate carboxylase protein was in the form of holoenzyme than in the cells growing on glucose under biotin limitation. The existence of urea amidolyase apoprotein in yeast cells grown with urea as the sole nitrogen source under biotin deficiency is reported. The presence of acetyl-CoA apocarboxylase in biotin-deficient cells could not be demonstrated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00411350
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  • 5
    Electronic Resource
    Electronic Resource
    Characterization of peroxisomes in glucose-grown Hansenula polymorpha and their development after the transfer of cells into methanol-containing media (1979)
    Springer
    Archives of microbiology 120 (1979), S. 167-175 
    Details
    ISSN: 1432-072X
    Keywords: Peroxisome ; Biogenesis ; Yeast ; Hansenula polymorpha ; Cytochemical staining ; Methanol
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cells of Hansenula polymorpha growing exponentially on glucose generally contained a single peroxisome of small dimension, irregular in shape and located in close proximity to the cell wall. Crystalline inclusions in the peroxisomal matrix were not observed. Associations of the organelles with one or more strands of endoplasmic reticulum were evident. In stationary phase cells the size of the peroxisomes had increased considerably. They were more cubical in form and showed a partly or completely crystalline matrix. After the transfer of cells growing exponentially on glucose into media containing methanol, large peroxisomes with a partly crystalline matrix developed in the cells within 6 h. These organelles originated from the small peroxisomes in the glucose-grown cells. De novo synthesis of peroxisomes was not observed. Prolonged cultivation in the presence of methanol resulted in a gradual increase in the number of peroxisomes by means of separation of small peroxisomes from mature organelles. During growth of peroxisomes associations with the endoplasmic reticulum remained evident. The increase in volume density of peroxisomes in stationary phase cells grown on glucose and in methanol-grown cells was accompanied by the synthesis of the peroxisomal enzymes alcohol oxidase and catalase. Cytochemical staining techniques revealed that alcohol oxidase activity was only detected when the peroxisomes contained a crystalloid inclusion. Since in peroxisomes of an alcohol oxidase-negative mutant of Hansenula polymorpha crystalline inclusions were never detected, it is concluded that the development of crystalloids inside peroxisomes is due to the accumulation of alcohol oxidase in these organelles.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00409104
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  • 6
    Electronic Resource
    Electronic Resource
    Differential extraction of soluble pools from the cytosol and the vacuoles of yeast (Candida utilis) using DEAE-dextran (1979)
    Springer
    Archives of microbiology 120 (1979), S. 141-149 
    Details
    ISSN: 1432-072X
    Keywords: Yeast ; DEAE-dextran ; Compartmentation ; Vacuoles ; Cytosol ; Amino acids ; Ions
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The plasma membrane of Candida utilis cells was rapidly disrupted by a small dose of DEAE-dextran. The vacuolar membranes, in contrast, remained intact under isotonic conditions. Therefore, the cytosolic pool could be extracted in a first step, and in a second step, after disruption of the vacuoles, the vacuolar pool. The two extracts were studied in cells grown on different nitrogen sources, namely ammonium, arginine, ornithine, citrulline, glycine, and proline. The amount of soluble amino acids in Candida cells varies considerably depending on the nitrogen source. This is largely caused by the variation in size of the vacuolar pool (0.8–2.4 mmol per g protein) containing nearly all nitrogen-rich amino acids such as arginine and ornithine, whereas the size of the cytoplasmic pool, holding most of the glutamic acid, is fairly constant (1.3 mmol per g protein). Upon nitrogen starvation the vacuolar pool was reduced much more than the cytosolic pool. A storage and buffer function of the vacuolar pool was also indicated by the much slower turnover of the vacuolar than of the cytosolic glutamine in an isotope labelling experiment. Potassium, sodium, orthophosphate, ATP, and other substances absorbing at 260 nm were found predominantly in the cytosolic extracts. Extraction of uniformly 14C-labelled cells showed that the total soluble pool of the cells contained about 10% of the total carbon. Of this about 45% was in the vacuolar the rest in the cytosolic extract. The labelled extracts were further characterized by ion exchange chromatography.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00409100
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