| | 3 | Author
| Bemd Schulz-Harder, Claudia Kiicherer | Requires cookie* | | | Title
| in Saccharomyces cerevisiae  | | | | Abstract
| The ribosomal ribonuclease of yeast is induced after a withdrawal of glucose. Cycloheximide inhibits the synthesis of the enzyme under conditions of induction but antimycin shows no effect. Hence, the increase of the ribonuclease activity during growth of yeast is due to newly synthesized enzyme, and the induction does not depend on respiration. | | | |
Reference
| Z. Naturforsch. 35c, 168—170 (1980); received February 13/September 5 1979 | | | |
Published
| 1980 | | | |
Keywords
| Yeast, Ribosomes, Ribonuclease, Cycloheximide, Antimycin | | | |
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| default:Reihe_C/35/ZNC-1980-35c-0168_n.pdf | | | | Identifier
| ZNC-1980-35c-0168_n | | | | Volume
| 35 | |
| 4 | Author
| Bernd Schulz-Harder, Ernst-Randolf Lochmann | Requires cookie* | | | Title
| Initiation in einem Polyribosomen-abhängigen Protein-synthetisierenden zellfreien System aus Saccharomyces Initiation in a Polyribosome-Dependent Protein-Synthesizing Cell-Free System from Saccharomyces | | | | Abstract
| A method to prepare polyribosomes from yeasts by using the french-press is described. The highest yield of polyribosomes was derived from late log-phase cells. These polyribosomes, in cubated in a cell-free system, were able to reinitiate protein synthesis, which was shown by in hibiting aminoacid incorporation by aurintricarboxylic acid, edeine and sodiumfluoride. W e de veloped the translational system in order to look for the optimal ion-conditions of a DNA-dependent protein-synthesizing system. W e found out that at the optimal MgCL-concentration (6 mM) protein synthesis was strongly inhibited by Mangan ions which are required for transcription in yeast. If protein-synthesis was carried out with 2 mM and 3 mM M gCU maximal aminoacid incorporation was observed at 2 mM and 1.5 mM M nCl2 . | | | |
Reference
| (Z. Naturforsch. 31c, 169 [1976]; eingegangen am 10. November 1975) | | | |
Published
| 1976 | | | |
Keywords
| Yeast, Polyribosomes, Cell-Free Protein Synthesis, Antibiotics, Ion-Conditions | | | |
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| default:Reihe_C/31/ZNC-1976-31c-0169.pdf | | | | Identifier
| ZNC-1976-31c-0169 | | | | Volume
| 31 | |
| 5 | Author
| Brigitte Kiefer, Laske | Requires cookie* | | | Title
| Jürgen | | | | Abstract
| Protein synthesis after UV-and X-irradiation was investigated in diploid yeast. The incorpora tion of radioactively labelled lysine and phenylalanine was measured 2.5 and 4 hours after ex posure. By varying the specific activity the pool sizes could be estimated. At 2.5 hours there is some increase in pool sizes and a dose-dependent enhancement of protein synthesis. At 4 hours pools are again normal, but the increase of synthetic activity prevails. | | | |
Reference
| (Z. Naturforsch. 32c, 973 [1977]; received August 29 1977) | | | |
Published
| 1977 | | | |
Keywords
| Yeast, Protein Synthesis, Amino Acid Pools, Irradiation | | | |
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| default:Reihe_C/32/ZNC-1977-32c-0973.pdf | | | | Identifier
| ZNC-1977-32c-0973 | | | | Volume
| 32 | |
| 6 | Author
| J.F T Spencer, DorothyM. Spencer | Requires cookie* | | | Title
| Osmotic Sensitivity and Tolerance and Proteinase Production in a Strain of Saccharomyces | | | | Abstract
| A brewing yeast strain, NCYC 1085, unusual in that it sporulated freely and produced diploid spores, was sensitive to the degree of osmotic tension induced by the addition of 1.5 M KC1 or 2.5 m ethylene glycol to yeast extract-peptone-glucose medium, but its progeny, obtained on sporula-tion and dissection of the resulting asci, included a number of osmotic-tolerant strains, the per centage of which increased as these strains were also sporulated and dissected. In addition, after repeated isolation of single-spore clones for three or four generations, clones producing zones of liquefaction of gelatin ranging in size from zero to large (approximately 1.5 cm) appeared, with the intensity of hydrolysis increasing in clones obtained from the later generations. The isolation of erythromycin-resistant mutants by manganese treatment was also accompanied by the appearance of osmotic-tolerant and gelatin-liquefying clones. | | | |
Reference
| Z. Naturforsch. 34c, 131 (1979); received November 5 1978 | | | |
Published
| 1979 | | | |
Keywords
| Yeast, Saccharom yces, Extracellular Proteases, Genetics, Osmotolerance | | | |
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| default:Reihe_C/34/ZNC-1979-34c-0131.pdf | | | | Identifier
| ZNC-1979-34c-0131 | | | | Volume
| 34 | |
| 7 | Author
| Maja Mischel, Ingolf Lam | Requires cookie* | | | Title
| Dielectrophoretic Rotation in Budding Yeast Cells | | | | Abstract
| Rotation of budding yeast cells in an alternating non-uniform electric field of low frequency was investigated. Rotation frequency was found to be proportional to field strength above a threshold, and varied from cell to cell. The threshold is inversely correlated with the mom ent of inertia of the cells, while the slope of rotation frequency versus field strength increases with the moment. Rotation frequencies varied between 1 and 10 cycles per second. Clear differences between the dielectrophoretic behaviour o f living and heat-inactivated yeast cells were observed. | | | |
Reference
| Z. Naturforsch. 35c, 1111 (1980); received July 21/Septem ber 10 1980 | | | |
Published
| 1980 | | | |
Keywords
| Dielectrophoresis, Rotation, Yeast, N onuniform Electric Fields | | | |
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| | | | | TEI-XML for
| default:Reihe_C/35/ZNC-1980-35c-1111_n.pdf | | | | Identifier
| ZNC-1980-35c-1111_n | | | | Volume
| 35 | |
| 8 | Author
| Christian Kreutzfeldt | Requires cookie* | | | Title
| Initiation of Protein Synthesis in Yeast: Binding of Met-tRNAj | | | | Abstract
| Conditions for the binding of Met-tRNAj to 40 s ribosomal subunits and to proteins isolated out o f the yeast ribosomal KC1 wash were investigated. Sucrose density gradient experiments revealed that binding of Met-tRNAj to 40 s ribosomal subunits was catalyzed in a AUG and GTP dependent reaction. Binding of Met-tRNAi to proteins of the ribosomal KC1 wash as assayed by the Millipore filter technique was found to be independent of AUG, GTP and 40 s ribosomal subunits. Additions of GTP yielded only slight stimulation, whereas Mg2+ caused dissociation of complexes. It was concluded that these reactions were most likely catalyzed by initiation factor eIF-2 although stimulation by GTP did not occur. | | | |
Reference
| Z. Naturforsch. 36c, 142—148 (1981); received September 18 1980 | | | |
Published
| 1981 | | | |
Keywords
| Protein Synthesis, Initiation, Initiator tRNA, Yeast | | | |
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| default:Reihe_C/36/ZNC-1981-36c-0142.pdf | | | | Identifier
| ZNC-1981-36c-0142 | | | | Volume
| 36 | |
| 9 | Author
| Hans-Jürgen Schuetz, H. Elm, Ut Simon | Requires cookie* | | | Title
| Degradation of NAD(H ) by Endogenous Enzymes of Yeasts and Clostridia | | | | Abstract
| The time courses of degradation of exogenous NAD and NADH (2.5 m M) catalyzed by en dogenous enzymes present in Saccharom yces cerevisiae, Candida utilis, Clostridium spec. La 1, C lostridium kluyveri, and Clostridium sporogenes have been determined. The half lives of the pyridine nucleotides depend extremely on the organism and, for the same organism, on the growth conditions. C. spec. La 1 as well as C. kluyveri possess only negligible enzyme activities for NAD degradation. However, C. sporogenes shows activities leading to half lives of less than 2 h for NAD and 5 h for NADH. At 25 °C half lives in the order of 5 — 17 h have been observed for Candida utilis under different conditions. The half lives of NAD are roughly 5 times higher in the presence of Saccharom yces cerevisiae. | | | |
Reference
| Z. Naturforsch. 41c, 172—178 (1986); received July 25. 1985 | | | |
Published
| 1986 | | | |
Keywords
| NAD(H) Degradation, Clostridia, Yeasts, Bioconversion, Enzymatic Reductions | | | |
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| default:Reihe_C/41/ZNC-1986-41c-0172.pdf | | | | Identifier
| ZNC-1986-41c-0172 | | | | Volume
| 41 | |
| 10 | Author
| Susana Raquel, Correa Garcia, MariaVictoria Rossetti, Alcira Maria, Carmen Batlle, Porfirinas, Porfirias-C Ip, Y. P., N. Ic, E. T., F.C E, N. | Requires cookie* | | | Title
| Studies on Porphobilinogen-Deaminase from Saccharomyces cerevisiae | | | | Abstract
| Porphobilinogen-deaminase from Saccharomyces cerevisiae has been isolated and partially purified 80-and 230-fold in the absence or presence o f phenylmethylsulphonyl fluoride, re spectively. Some properties o f the isolated enzyme were studied. Porphyrin formation was linear with time and protein concentration. O ptim um pH was about 7.5-7.8. Molecular mass o f the pro tein was 30,000 ± 3000 Dalton when the enzyme was purified in the presence o f phenylmethyl sulphonyl fluoride. A less active and unstable 20,000 D a molecular mass species was obtained when purification was performed in the absence o f the protease inhibitor. Porphobilinogen-deaminase exhibited classical Michaelis-Menten kinetics. The apparent Ky for uroporphyrinogen formation was 19 hm; Fmax was 3.6 nmol uroporphyrin/h and the Hill coefficient was n = 1. Also the action o f several reagents on the activity was studied. Protective thiol agents had no effect. Heavy metals inhibited both porphyrin formation and porphobilinogen consumption, but known sulphydryl inactivating chemicals inhibit the former without modifying the latter. A m m o nium ions had no effect on the activity while hydroxylamine completely inhibited both porphyrin form ation and porphobilinogen consumption. | | | |
Reference
| Z. Naturforsch. 46c, 1017—1023 (1991); received December 17 1990/May 27 1991 | | | |
Published
| 1991 | | | |
Keywords
| Saccharomyces cerevisiae, Yeast, Porphobilinogen-Deaminase, Porphyrin Biosynthesis, Porphobilinogen | | | |
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| default:Reihe_C/46/ZNC-1991-46c-1017.pdf | | | | Identifier
| ZNC-1991-46c-1017 | | | | Volume
| 46 | |
| 11 | Author
| G. Alina Lazarova, Tam Otsu, O. Otaki, Kunio Isono, H. Ironao, K. Ataoka | Requires cookie* | | | Title
| Phototropism in Yeast: A New Phenomenon to Explore Blue Light-Induced Responses | | | | Abstract
| Although yeasts have been intensively investigated in photobiology, directional response of yeast growth to light has never been observed. The present data demonstrate for the first time phototropism in yeast, the basidiomycetous yeast Sporobolomyces salmonicolor. The effective spectral band is blue light -suggesting that a blue-light receptor similar to that in other plants is involved in yeast photophysiology. Further studies on yeast phototropism could help identification of the photoreceptor and throw new light on the mechanisms of signal transduction and response. | | | |
Reference
| Z. Naturforsch. 49c, 751—756 (1994); received July 19 1994 | | | |
Published
| 1994 | | | |
Keywords
| Phototropism, Yeast, Sporobolomyces salmonicolor, Blue Light | | | |
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| default:Reihe_C/49/ZNC-1994-49c-0751.pdf | | | | Identifier
| ZNC-1994-49c-0751 | | | | Volume
| 49 | |
| 12 | Author
| M. Auro, Sola-Pennaa, JoseR. Oberto, M. Eyer-Fernandesb | Requires cookie* | | | Title
| Trehalose Protects Yeast Pyrophosphatase against Structural and Functional Damage Induced by Guanidinium Chloride | | | | Abstract
| Trehalose is accumulated at very high concentrations in yeasts when this organism is sub mitted to a stress condition. This report approaches the question on the protective effect of trehalose and its degradation product, glucose, against structural and functional damage promoted by guanidinium on yeast cytosolic pyrophosphatase. Here it is shown that both, 1 m trehalose or 2 m glucose, are able to attenuate at almost the same extent the conforma tional changes promoted by guanidinium chloride on the pyrophosphatase structure. On the other hand, while 1 m trehalose increases 3.8 times the K x (from 0.15 to 0.57 m) for guanidi nium chloride inhibition of pyrophosphatase activity, 2 m glucose did not even duplicate this parameter (from 0.15 to 0.25 m). These data support evidences for a functional reason for the accumulation by yeasts of trehalose, and not other compound, during stress conditions. | | | |
Reference
| Z. Naturforsch. 51c, 160—164 (1996); received September 15/November 15 1995 | | | |
Published
| 1996 | | | |
Keywords
| Trehalose, Yeast, Carbohydrate, Protection, Guanidinium Chloride | | | |
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| default:Reihe_C/51/ZNC-1996-51c-0160.pdf | | | | Identifier
| ZNC-1996-51c-0160 | | | | Volume
| 51 | |
| 13 | Author
| Hans Eckstein, Sybille Ahnefeld, Karin Albietz-Loges | Requires cookie* | | | Title
| Synthesis of Deoxynucleoside Tri-and Monophosphates in Synchronized and Asynchronously Growing Cells Acid-Soluble Deoxynucleotides and DNA Synthesis in Growing Yeast after X-Irradiation, II | | | | Abstract
| The behaviour of acid-soluble D NA precursors in synchronized and asynchronously growing yeast after X-irradiation is investigated by labeling techniques with 32P; and by enzymic estimation. In prelabeled synchronized growing cells, radioactivity associated with deoxynucleoside triphos phates increases to maximum values shortly before each DNA replication, followed by a drastic decrease during S-phase. Radioactivity associated with monophosphates fluctuates, too, but with an opposite rhythm. These fluctuations apparently reflect quantitative changes of the DNA precursor pool during a cell cycle, as judged from the following findings: 1. Acid-soluble phosphorus is augmented stepwise. 2. "Specific" radioactivity from acid-soluble phosphorus compounds de creases steadily, indicating a continuous dilution of the labeled phosphorus pool with "cold" phos phorus. 3. Radioactivity associated with ribonucleotides fluctuates, too, but with a divergent rhythm. In X-irradiated synchronice growing yeast, the fluctuations of the deoxynucleotide-associated 32P are disturbed only little. Maximum values appear nearly at the same time as in the control, they decrease to minor values even if D NA augmentation is delayed. This decrease is less drastic, however, than that during DNA replication in unirradiated yeast, yielding a slightly increased aver age label per generation time. At the same sime a rapid augmentation of monophosphate label is observed. A pronounced increase of deoxynucleotide-32P is seen with X-irradiated asynchronously growing yeast, pointing to distinct radiosensitivities of the D N A /D N A precursor system in different cell stages. Neither 32P-fluctuations nor 32P-accumulation during DNA delay can be explained by cor responding observations with acid-soluble phosphorus or with ribonucleotide pools. Studies on 32P-incorporation also exclude radiation effects on cellular phosphorus uptake. Enzymic estimations of the deoxynucleoside triphosphate pools from asynchronously growing yeast rather exhibit a con siderable increase of these substances during the radiation-induced delay of DNA augmentation. This accumulation of DNA precursors probably is caused by undisturbed synthesis, but reduced incorporation into DNA. The possible role of D NA repair in this system is discussed. | | | |
Reference
| (Z. Naturforsch. 29c, 272 [1974]; received January 17 1974) | | | |
Published
| 1974 | | | |
Keywords
| Deoxynucleoside Triphosphates, Deoxynucleoside Monophosphates, Yeast, X-Irradiation, Phosphorus Turnover | | | |
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| default:Reihe_C/29/ZNC-1974-29c-0272.pdf | | | | Identifier
| ZNC-1974-29c-0272 | | | | Volume
| 29 | |
| 14 | Author
| Stefan Postius | Requires cookie* | | | Title
| In vivo Evidence for a Functional Glycolytic Compartment in Synchronous Yeast Cells | | | | Abstract
| The different metabolic behaviour of endogenously produced [1-14C] pyruvate derived from [3,4-14C]glucose and of exogenously added [1-14C]pyruvate were studied with synchronous yeast cell populations, under conditions which differentially influenced the activities o f pyruvate decarboxylase in the cytoplasm and pyruvate dehydrogenase in the mitochondria. Endogenously produced [1-14C]pyruvate is decarboxylated almost exclusively by PDC under anaerobic condi tions, in contrast to added [1-14C]pyruvate which is decarboxylated under aerobic conditions by the action of PDH mainly. Whereas 14C 0 2 evolution from exogenous [l-14C]pyruvate can be diluted proportionally by addition o f pyruvate, this is not the case for 14C 0 2 evolution from endogenous [1-14C]pyruvate. It is suggested that glycolysis or at least some constituents o f it might be arranged in such a manner that the resulting complex behaves as a functional compartment, meaning that it is almost inaccessible to exogenously added pyruvate. | | | |
Reference
| Z. Naturforsch. 36c, 615—6 (1981); received November 20 1980/January 28 1981 | | | |
Published
| 1981 | | | |
Keywords
| Continuous 14C 0 2 Evolution, Glycolytic Compartment, Pyruvate Metabolism, Synchronous, Yeast | | | |
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| | | | | TEI-XML for
| default:Reihe_C/36/ZNC-1981-36c-0615.pdf | | | | Identifier
| ZNC-1981-36c-0615 | | | | Volume
| 36 | |
| 16 | Author
| Hans-Peter Hanssen, Ewald Sprecher, AndreasK. Lingenberg | Requires cookie* | | | Title
| Accumulation of Volatile Flavour Compounds in Liquid Cultures of Kluyveromyces lactis Strains | | | | Abstract
| The accumulation o f volatile flavour constituents in liquid cultures o f three Kluyverom yces lactis strains was studied after cultivation on defined culture m edia containing glucose as carbon source, yeast extract, vitamines, and different additional nitrogen com pounds. Besides short-chain alcohols and esters (fruit esters), 2-phenylethyl alcohol, phenylacetaldehyde, and 2-phenylethyl esters could be identified by gas chrom atography and coupled gas chrom atog-raphy-mass spectrometry. Although the com position o f these com pounds was qualitatively comparable within the three strains investigated, quantitative differences were significant and strain-dependent reactions to the culture m edium could be observed. | | | |
Reference
| Z. Naturforsch. 39c, 1030—1033 (1984); received July 2/A ugust 28 1984 | | | |
Published
| 1984 | | | |
Keywords
| Kluyveromyces lactis, Yeast, Volatiles, Flavour Com pounds, Culture C onditions | | | |
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| default:Reihe_C/39/ZNC-1984-39c-1030.pdf | | | | Identifier
| ZNC-1984-39c-1030 | | | | Volume
| 39 | |
| 17 | Author
| G. Ünter Müller, W. Olfhard Bandlow | Requires cookie* | | | Title
| cA M P-Dependent Protein Kinase Activity in Yeast Mitochondria | | | | Abstract
| Two different cAMP-binding proteins have been identified in yeast mitochondria by photo affinity labelling and based on the occurrence of cAMP-binding activity in two different sub-mito chondrial fractions. One protein (M r 45—46000) is tightly bound to the inner mitochondrial membrane whereas the other (M r 42000) is found in the soluble intermembrane space. With endogenous substrate cAMP-dependent protein kinase activity could not be demonstrated with sufficient clarity. However, using acidic heterologous substrates, like casein and phosvitin, one cAMP-dependent protein kinase was identified in the intermembrane space. Only low phosphate incorporation was found using histone fractions as substrate. cAMP-dependent modification of proteins appears to be very shortlived in mitochondria. Its physiological significance remains unknown, since neither mitochondrial transcription, translation, respiration nor import of cyto-plasmically synthesized precursors into mitochondria appear to be influenced by exogenous cAMP either in vivo or in vitro. It is shown that cAMP is not actively transported into the inner mitochondrial compartment but rather binds to a receptor(s) localized outside the permeability barrier provided by the inner membrane. | | | |
Reference
| Z. Naturforsch. 42c, 1291 (1987); received May 29/August 3. 1987 | | | |
Published
| 1987 | | | |
Keywords
| cAMP-Dependent Protein Kinase, Protein Phosphatase, Yeast, Mitochondria, Sub-Mitochon-drial Location | | | |
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| default:Reihe_C/42/ZNC-1987-42c-1291.pdf | | | | Identifier
| ZNC-1987-42c-1291 | | | | Volume
| 42 | |
| 18 | Author
| Hans Eckstein | Requires cookie* | | | Title
| Evidence for Cyclic GMP in the Yeast Saccharomyces cerevisiae, and Studies on Its Possible Role in Growth | | | | Abstract
| The yeast Saccharomyces cerevisiae is shown to be equipped with cyclic GMP, the level of which ranges from 6 pmol/10 9 cells with pressed baker's yeast to 21 pmol/10 9 cells with exponentially growing cells. In extracts from synchronized growing yeast, cyclic GMP increases stepwise, being doubled at the time of each mitosis. Theophylline and 3-isobutyl-l-methylxanthine induce a rapid increase of cyclic GMP, followed by a premature formation of the septal cell wall between mother cell and bud. The effects of 3-isobutyl-l-methylxanthine are reversible. Dibutyryl-cyclic GMP, and, after a pronounced lag, also dibutyryl-cyclic AMP, induce a premature cell division, too. Cholera toxin induces premature cell divisions without a preceding increase in cyclic GMP. Neither theophylline nor 3-isobutyl-l-methylxanthine, cholera toxin or one of the dibutyryl-cyclic nucleotides modify the growth rate of the culture. None of the agents has significant effects on the level of cyclic AMP. The results suggest that cyclic GMP possibly controls an early step of mitosis, whereas ADP-ribosylation might govern a subsequent event. | | | |
Reference
| Z. Naturforsch. 43c, 386—396 (1988); received October 20 1987 | | | |
Published
| 1988 | | | |
Keywords
| Cyclic GMP, Cyclic AMP, Phosphodiesterase Inhibitors, Cholera Toxin, Growth, Yeast | | | |
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| | | | | TEI-XML for
| default:Reihe_C/43/ZNC-1988-43c-0386.pdf | | | | Identifier
| ZNC-1988-43c-0386 | | | | Volume
| 43 | |
|
