Background: In Saccharomyces cerevisiae, the retrograde signalling pathway is activated in \u03c1^{0/- cells, which lack mitochondrial DNA. Within this pathway, the activation of the transcription factor Pdr3 induces transcription of the ATP-binding cassette (ABC) transporter gene, PDR5, and causes pleiotropic drug resistance (PDR). Although a histone deacetylase, Rpd3, is also required for cycloheximide resistance in \u03c10/- cells, it is currently unknown whether Rpd3 and its DNA binding partners, Ume6 and Ash1, are involved in the activation of PDR5 transcription and PDR in \u03c10/- cells. This study investigated the roles of RPD3, UME6, and ASH1 in the activation of PDR5 transcription and PDR by retrograde signalling in \u03c10 cells.}

Results: \u03c1^{0 cells in the rpd3\u2206 and ume6\u2206 strains, with the exception of the ash1\u2206 strain, were sensitive to fluconazole and cycloheximide. The} PDR5 mRNA levels in \u03c1^{0 cells of the rpd3\u2206 and ume6\u2206 strains were significantly reduced compared to the wild-type and ash1\u2206 strain. Transcriptional expression of} PDR5 was reduced in cycloheximide-exposed and unexposed \u03c1^{0 cells of the ume6\u2206 strain; the transcriptional positive response of} PDR5 to cycloheximide exposure was also impaired in this strain.

Conclusions: RPD3 and UME6 are responsible for enhanced PDR5 mRNA levels and PDR by retrograde signalling in \u03c1^{0 cells of S. cerevisiae."}, "year": 2021, "reftypes": [{"display_name": "Journal Article"}, {"display_name": "Research Support, Non-U.S. Gov't"}], "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1186/s12866-021-02373-1"}, {"display_name": "PMC full text", "link": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8576940/"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/34753419"}]}, {"id": 2093507, "display_name": "Hasegawa S, et al. (2019)", "link": "/reference/S000247483", "citation": "Hasegawa S, et al. (2019) Identification and functional characterization of Candida albicans mannose-ethanolamine phosphotransferase (Mcd4p). Curr Genet 65(5):1251-1261", "pubmed_id": 31073667, "abstract": {"text": "Glycosylphosphatidylinositol (GPI) is an important compound for the growth of fungi, because GPI-anchored proteins including glycosyltransferases and adhesins are involved in cell-wall integrity, adhesion, and nutrient uptake in this organism. In this study, we examined orf19.5244 in the genome database of the pathogenic fungus Candida albicans, a homologue of the Saccharomyces cerevisiae mannose-ethanolamine phosphotransferase gene,} MCD4, which plays a role in GPI synthesis. Expression of this homologue, designated CaMCD4, restored cell growth in a defective conditional MCD4 mutant of S. cerevisiae, ScMCD4t, in which expression of native MCD4 was repressed in the presence of doxycycline (Dox). Analysis of radiolabeled lipids showed that the accumulation of abnormal GPI anchor precursors in ScMCD4t decreased markedly upon expression of CaMCD4. Moreover, we constructed a single mutant (CaMCD4/CaMCD4) and a conditional double mutant (CaMCD4/CaMCD4t) at the MCD4 locus of C. albicans. Repression of CaMCD4 expression by Dox led to a decrease in growth and appearance of abnormal morphology in C. albicans, both in vitro and in a silkworm infection model. These results suggest that CaMcd4p is indispensable for growth of C. albicans both in vitro and in infected hosts and a candidate target for the development of new antifungals."}, "year": 2019, "reftypes": [{"display_name": "Journal Article"}], "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1007/s00294-019-00987-7"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/31073667"}]}, {"id": 391210, "display_name": "Yamada Y, et al. (2012)", "link": "/reference/S000152186", "citation": "Yamada Y, et al. (2012) Validation of MIMGO: a method to identify differentially expressed GO terms in a microarray dataset. BMC Res Notes 5:680", "pubmed_id": 23232071, "abstract": {"text": "

Background: We previously proposed an algorithm for the identification of GO terms that commonly annotate genes whose expression is upregulated or downregulated in some microarray data compared with in other microarray data. We call these \"differentially expressed GO terms\" and have named the algorithm \"matrix-assisted identification method of differentially expressed GO terms\" (MIMGO). MIMGO can also identify microarray data in which genes annotated with a differentially expressed GO term are upregulated or downregulated. However, MIMGO has not yet been validated on a real microarray dataset using all available GO terms.

Findings: We combined Gene Set Enrichment Analysis (GSEA) with MIMGO to identify differentially expressed GO terms in a yeast cell cycle microarray dataset. GSEA followed by MIMGO (GSEA + MIMGO) correctly identified (p < 0.05) microarray data in which genes annotated to differentially expressed GO terms are upregulated. We found that GSEA + MIMGO was slightly less effective than, or comparable to, GSEA (Pearson), a method that uses Pearson's correlation as a metric, at detecting true differentially expressed GO terms. However, unlike other methods including GSEA (Pearson), GSEA + MIMGO can comprehensively identify the microarray data in which genes annotated with a differentially expressed GO term are upregulated or downregulated.

Conclusions: MIMGO is a reliable method to identify differentially expressed GO terms comprehensively."}, "year": 2012, "reftypes": [{"display_name": "Journal Article"}, {"display_name": "Research Support, Non-U.S. Gov't"}, {"display_name": "Validation Study"}], "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1186/1756-0500-5-680"}, {"display_name": "PMC full text", "link": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3557167/"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/23232071"}]}, {"id": 508626, "display_name": "Yamada Y, et al. (2007)", "link": "/reference/S000120367", "citation": "Yamada Y, et al. (2007) The crystal structure of Atg3, an autophagy-related ubiquitin carrier protein (E2) enzyme that mediates Atg8 lipidation. J Biol Chem 282(11):8036-43", "pubmed_id": 17227760, "abstract": {"text": " Atg3 is an E2-like enzyme that catalyzes the conjugation of Atg8 and phosphatidylethanolamine (PE). The Atg8-PE conjugate is essential for autophagy, which is the bulk degradation process of cytoplasmic components by the vacuolar/lysosomal system. We report here the crystal structure of Saccharomyces cerevisiae Atg3 at 2.5-A resolution. Atg3 has an alpha/beta-fold, and its core region is topologically similar to canonical E2 enzymes. Atg3 has two regions inserted in the core region, one of which consists of approximately 80 residues and has a random coil structure in solution and another with a long alpha-helical structure that protrudes from the core region as far as 30 A. In vivo and in vitro analyses suggested that the former region is responsible for binding Atg7, an E1-like enzyme, and that the latter is responsible for binding Atg8. A sulfate ion was bound near the catalytic cysteine of Atg3, suggesting a possible binding site for the phosphate moiety of PE. The structure of Atg3 provides a molecular basis for understanding the unique lipidation reaction that Atg3 carries out."}, "year": 2007, "reftypes": [{"display_name": "Journal Article"}, {"display_name": "Research Support, Non-U.S. Gov't"}], "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1074/jbc.M611473200"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/17227760"}]}, {"id": 524666, "display_name": "Satoh T, et al. (2006)", "link": "/reference/S000114286", "citation": "Satoh T, et al. (2006) Structures of the carbohydrate recognition domain of Ca2+-independent cargo receptors Emp46p and Emp47p. J Biol Chem 281(15):10410-9", "pubmed_id": 16439369, "abstract": {"text": " Emp46p and Emp47p are type I membrane proteins, which cycle between the endoplasmic reticulum (ER) and the Golgi apparatus by vesicles coated with coat protein complexes I and II (COPI and COPII). They are considered to function as cargo receptors for exporting N-linked glycoproteins from the ER. We have determined crystal structures of the carbohydrate recognition domains (CRDs) of Emp46p and Emp47p of Saccharomyces cerevisiae, in the absence and presence of metal ions. Both proteins fold as a beta-sandwich, and resemble that of the mammalian ortholog, p58/ERGIC-53. However, the nature of metal binding is distinct from that of Ca(2+)-dependent p58/ERGIC-53. Interestingly, the CRD of Emp46p does not bind Ca(2+) ion but instead binds K(+) ion at the edge of a concave beta-sheet whose position is distinct from the corresponding site of the Ca(2+) ion in p58/ERGIC-53. Binding of K(+) ion to Emp46p appears essential for transport of a subset of glycoproteins because the Y131F mutant of Emp46p, which cannot bind K(+) ion fails to rescue the transport in disruptants of EMP46 and EMP47 genes. In contrast the CRD of Emp47p binds no metal ions at all. Furthermore, the CRD of Emp46p binds to glycoproteins carrying high mannosetype glycans and the is promoted by binding not the addition of Ca(2+) or K(+) ion in These results suggest that Emp46p can be regarded as a Ca(2+)-independent intracellular lectin at the ER exit sites."}, "year": 2006, "reftypes": [{"display_name": "Journal Article"}, {"display_name": "Research Support, Non-U.S. Gov't"}], "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1074/jbc.M512258200"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/16439369"}]}, {"id": 511990, "display_name": "Yamada Y, et al. (2006)", "link": "/reference/S000119096", "citation": "Yamada Y, et al. (2006) Crystallization and preliminary X-ray analysis of Atg3. Acta Crystallogr Sect F Struct Biol Cryst Commun 62(Pt 10):1016-7", "pubmed_id": 17012800, "abstract": {"text": " Atg3 is an E2-like enzyme that catalyzes the conjugation reaction between Atg8 and phosphatidylethanolamine (PE). The Atg8-PE conjugate is essential for autophagy, the bulk degradation process of cytoplasmic components by the vacuolar/lysosomal system. Crystals of Saccharomyces cerevisiae Atg3 have been obtained by the sitting-drop vapour-diffusion method using ammonium sulfate and lithium sulfate as precipitants. A native data set was collected from a single crystal to 2.5 A resolution. The crystals belong to space group P4(1) or P4(3), with unit-cell parameters a = 59.33, c = 115.22 A, and are expected to contain one protein molecule per asymmetric unit."}, "year": 2006, "reftypes": [{"display_name": "Journal Article"}, {"display_name": "Research Support, Non-U.S. Gov't"}], "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1107/S1744309106036098"}, {"display_name": "PMC full text", "link": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2225171/"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/17012800"}]}, {"id": 555314, "display_name": "Yamada Y, et al. (2002)", "link": "/reference/S000072079", "citation": "Yamada Y, et al. (2002) The 2.0 A crystal structure of catalase-peroxidase from Haloarcula marismortui. Nat Struct Biol 9(9):691-5", "pubmed_id": 12172540, "abstract": {"text": "Catalase-peroxidase is a member of the class I peroxidase superfamily. The enzyme exhibits both catalase and peroxidase activities to remove the harmful peroxide molecule from the living cell. The 2.0 A crystal structure of the catalase-peroxidase from Haloarcula marismortui (HmCP) reveals that the enzyme is a dimer of two identical subunits. Each subunit is composed of two structurally homologous domains with a topology similar to that of class I peroxidase. The active site of HmCP is in the N-terminal domain. Although the arrangement of the catalytic residues and the cofactor heme b in the active site is virtually identical to that of class I peroxidases, the heme moiety is buried inside the domain, similar to that in a typical catalase. In the vicinity of the active site, novel covalent bonds are formed among the side chains of three residues, including that of a tryptophan on the distal side of the heme. Together with the C-terminal domain, these covalent bonds fix two long loops on the surface of the enzyme that cover the substrate access channel to the active site. These features provide an explanation for the dual activities of this enzyme."}, "year": 2002, "reftypes": [{"display_name": "Journal Article"}, {"display_name": "Research Support, Non-U.S. Gov't"}], "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1038/nsb834"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/12172540"}]}, {"id": 574079, "display_name": "Byl JA, et al. (2001)", "link": "/reference/S000065474", "citation": "Byl JA, et al. (2001) DNA topoisomerase II as the target for the anticancer drug TOP-53: mechanistic basis for drug action. Biochemistry 40(3):712-8", "pubmed_id": 11170388, "abstract": {"text": "TOP-53 is a promising anticancer agent that displays high activity against non-small cell lung cancer in animal tumor models [Utsugi, T., et al. (1996) Cancer Res. 56, 2809-2814]. Compared to its parent compound, etoposide, TOP-53 is considerably more toxic to non-small cell lung cancer cells, is more active at generating chromosomal breaks, and displays improved cellular uptake and pharmacokinetics in animal lung tissues. Despite the preclinical success of TOP-53, several questions remain regarding its cytotoxic mechanism. Therefore, this study characterized the basis for drug action. Results indicate that topoisomerase II is the primary cytotoxic target for TOP-53. Furthermore, the drug kills cells by acting as a topoisomerase II poison. TOP-53 exhibits a DNA cleavage site specificity that is identical to that of etoposide. Like its parent compound, the drug increases the number of enzyme-mediated DNA breaks by interfering with the DNA religation activity of the enzyme. TOP-53 is considerably more efficient than etoposide at enhancing topoisomerase II-mediated DNA cleavage and exhibits high activity against human topoisomerase IIalpha and IIbeta in vitro and in cultured cells. Therefore, at least in part, the enhanced cytotoxic activity of TOP-53 can be attributed to an enhanced activity against topoisomerase II. Finally, TOP-53 displays nearly wild-type activity against a mutant yeast type II enzyme that is highly resistant to etoposide. This finding suggests that TOP-53 can retain activity against systems that have developed resistance to etoposide, and indicates that substituents on the etoposide C-ring are important for topoisomerase II-drug interactions."}, "year": 2001, "reftypes": [{"display_name": "Journal Article"}, {"display_name": "Research Support, Non-U.S. Gov't"}, {"display_name": "Research Support, U.S. Gov't, P.H.S."}], "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1021/bi0021838"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/11170388"}]}, {"id": 418726, "display_name": "Kanaya S, et al. (1999)", "link": "/reference/S000144009", "citation": "Kanaya S, et al. (1999) Studies of codon usage and tRNA genes of 18 unicellular organisms and quantification of Bacillus subtilis tRNAs: gene expression level and species-specific diversity of codon usage based on multivariate analysis. Gene 238(1):143-55", "pubmed_id": 10570992, "abstract": {"text": "We examined codon usage in Bacillus subtilis genes by multivariate analysis, quantified its cellular levels of individual tRNAs, and found a clear constraint of tRNA contents on synonymous codon choice. Individual tRNA levels were proportional to the copy number of the respective tRNA genes. This indicates that the tRNA gene copy number is an important factor to determine in cellular tRNA levels, which is common with Escherichia coli and yeast Saccharomyces cerevisiae. Codon usage in 18 unicellular organisms whose genomes have been sequenced completely was analyzed and compared with the composition of tRNA genes. The 18 organisms are as follows: yeast S. cerevisiae, Aquifex aeolicus, Archaeoglobus fulgidus, B. subtilis, Borrelia burgdorferi, Chlamydia trachomatis, E. coli, Haemophilus influenzae, Helicobacterpylori, Methanococcusjannaschii, Methanobacterium thermoautotrophicum, Mycobacterium tuberculosis, Mycoplasma genitalium, Mycoplasma pneumoniae, Pyrococcus horikoshii, Rickettsia prowazekii, Synechocystis sp., and Treponema pallidum. Codons preferred in highly expressed genes were related to the codons optimal for the translation process, which were predicted by the composition of isoaccepting tRNA genes. Genes with specific codon usage are discussed in connection with their evolutionary origins and functions. The origin and terminus of replication could be predicted on the basis of codon usage when the usage was analyzed relative to the transcription direction of individual genes."}, "year": 1999, "reftypes": [{"display_name": "Journal Article"}, {"display_name": "Research Support, Non-U.S. Gov't"}], "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1016/s0378-1119(99)00225-5"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/10570992"}]}, {"id": 570762, "display_name": "Yamashita A, et al. (1999)", "link": "/reference/S000066655", "citation": "Yamashita A, et al. (1999) Structure of tropinone reductase-II complexed with NADP+ and pseudotropine at 1.9 A resolution: implication for stereospecific substrate binding and catalysis. Biochemistry 38(24):7630-7", "pubmed_id": 10387002, "abstract": {"text": "Tropinone reductase-II (TR-II) catalyzes the NADPH-dependent reduction of the carbonyl group of tropinone to a beta-hydroxyl group. The crystal structure of TR-II complexed with NADP+ and pseudotropine (psi-tropine) has been determined at 1.9 A resolution. A seven-residue peptide near the active site, disordered in the unliganded structure, is fixed in the ternary complex by participation of the cofactor and substrate binding. The psi-tropine molecule is bound in an orientation which satisfies the product configuration and the stereochemical arrangement toward the cofactor. The substrate binding site displays a complementarity to the bound substrate (psi-tropine) in its correct orientation. In addition, electrostatic interactions between the substrate and Glu156 seem to specify the binding position and orientation of the substrate. A comparison between the active sites in TR-II and TR-I shows that they provide different van der Waals surfaces and electrostatic features. These differences likely contribute to the correct binding mode of the substrates, which are in opposite orientations in TR-II and TR-I, and to different reaction stereospecificities. The active site structure in the TR-II ternary complex also suggests that the arrangement of the substrate, cofactor, and catalytic residues is stereoelectronically favorable for the reaction."}, "year": 1999, "reftypes": [{"display_name": "Journal Article"}], "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1021/bi9825044"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/10387002"}]}, {"id": 570759, "display_name": "Nakajima K, et al. (1998)", "link": "/reference/S000066656", "citation": "Nakajima K, et al. (1998) Crystal structures of two tropinone reductases: different reaction stereospecificities in the same protein fold. Proc Natl Acad Sci U S A 95(9):4876-81", "pubmed_id": 9560196, "abstract": {"text": "A pair of tropinone reductases (TRs) share 64% of the same amino acid residues and belong to the short-chain dehydrogenase/reductase family. In the synthesis of tropane alkaloids in several medicinal plants, the TRs reduce a carbonyl group of an alkaloid intermediate, tropinone, to hydroxy groups with different diastereomeric configurations. To clarify the structural basis for their different reaction stereospecificities, we determined the crystal structures of the two enzymes at 2.4- and 2.3-A resolutions. The overall folding of the two enzymes was almost identical. The conservation was not confined within the core domains that are conserved within the protein family but extended outside the core domain where each family member has its characteristic structure. The binding sites for the cofactor and the positions of the active site residues were well conserved between the two TRs. The substrate binding site was composed mostly of hydrophobic amino acids in both TRs, but the presence of different charged residues conferred different electrostatic environments on the two enzymes. A modeling study indicated that these charged residues play a major role in controlling the binding orientation of tropinone within the substrate binding site, thereby determining the stereospecificity of the reaction product. The results obtained herein raise the possibility that in certain cases different stereospecificities can be acquired in enzymes by changing a few amino acid residues within substrate binding sites."}, "year": 1998, "reftypes": [{"display_name": "Journal Article"}, {"display_name": "Research Support, Non-U.S. Gov't"}], "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1073/pnas.95.9.4876"}, {"display_name": "PMC full text", "link": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC20181/"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/9560196"}]}, {"id": 567436, "display_name": "Nanba H, et al. (1998)", "link": "/reference/S000067839", "citation": "Nanba H, et al. (1998) Isolation of Agrobacterium sp. strain KNK712 that produces N-carbamyl-D-amino acid amidohydrolase, cloning of the gene for this enzyme, and properties of the enzyme. Biosci Biotechnol Biochem 62(5):875-81", "pubmed_id": 9648217, "abstract": {"text": "Agrobacterium sp. strain KNK712, which produced N-carbamyl-D-amino acid amidohydrolase (DCase) was isolated from soil. The bacterium had D-specific hydantoinase activity also. Both enzymes are suitable for use in the production of D-amino acids. The DCase gene from Agrobacterium sp. strain KNK712 was cloned into Escherichia coli. The cloned DNA fragment contained one open reading frame, predicted to encode a peptide of 304 amino acids, with a calculated molecular weight of 34,285. The DCase gene was overexpressed under the control of the lac promoter, and DCase accounted for 50% of the soluble protein in the cells. The enzyme was purified and some properties were investigated. Both the optimum pH and the pH that gave greatest stability were about pH 7.0. The optimum temperature was 65 degrees C, and the enzyme was stable at 55 degrees C. The enzyme had strict specificity toward N-carbamyl-D-amino acids, and was inhibited by thiol reagents, Cu2+, Hg2+, Ag+, and ammonia."}, "year": 1998, "reftypes": [{"display_name": "Journal Article"}], "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1271/bbb.62.875"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/9648217"}]}, {"id": 616945, "display_name": "Anamnart S, et al. (1997)", "link": "/reference/S000050161", "citation": "Anamnart S, et al. (1997) The P-OLE1 gene of Pichia angusta encodes a delta 9-fatty acid desaturase and complements the ole1 mutation of Saccharomyces cerevisiae. Gene 184(2):299-306", "pubmed_id": 9031643, "abstract": {"text": "Three PCR-amplified DNA fragments hybridizing with the OLE1 gene encoding delta 9-fatty acid desaturase of Saccharomyces cerevisiae were obtained using, respectively, genomic DNAs of one strain each of Kluyveromyces thermotolerans, Pichia angusta and Yarrowia lipolytica as templates. A gene designated P-OLE1 was cloned from the above fragment of P. angusta and sequenced. An open reading frame of P-OLE1 encodes a 49.6-kDa protein consisting of 451 amino acid residues, which shows high identity (62%) and similarity (89%) to that deduced from the OLE1 nucleotide sequence. Expression of P-OLE1 driven by the S. cerevisiae GAP promoter or its own promoter complemented the ole1 mutation of S.cerevisiae. Transcription of P-OLE1 in the native host was suggested to be partially repressed by oleic acid in the medium, as was that of OLE1 in S. cerevisiae and a similar gene in Y. lipolytica, but that of a similar gene in K. thermotolerans was not."}, "year": 1997, "reftypes": [{"display_name": "Journal Article"}], "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1016/s0378-1119(96)00621-x"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/9031643"}]}, {"id": 649403, "display_name": "Fujimori K, et al. (1997)", "link": "/reference/S000039787", "citation": "Fujimori K, et al. (1997) Isolation and characterization of mutations affecting expression of the delta9- fatty acid desaturase gene, OLE1, in Saccharomyces cerevisiae. FEBS Lett 413(2):226-30", "pubmed_id": 9280286, "abstract": {"text": "Expression of the delta9- fatty acid desaturase gene, OLE1, of Saccharomyces cerevisiae is negatively regulated transcriptionally and post-transcriptionally by unsaturated fatty acids. In order to isolate mutants exhibiting irregulation of OLE1 expression, we constructed an OLE1p-PHO5 fusion gene as a reporter consisting of the PHO5 gene encoding repressible acid phosphatase (rAPase) under the control of the OLE1 promoter (OLE1p). By EMS mutagenesis, we isolated three classes of mutants, pfo1, pfo2 and pfo3 positive regulatory factor for OLE1) mutants, which show decreased rAPase activity under derepression conditions (absence of oleic acid). Analysis of the transcription of OLE1 in these pfo mutants revealed that pfo1 and pfo3 mutants have a defect in the regulation of OLE1 expression at the transcriptional level while pfo2 mutants were suggested to have a mutation affecting OLE1 expression at a post-transcriptional step. In addition, four other classes of mutants, nfo1, nfo2, nfo3 and nfo4 (negative factor for OLE1) mutants that have mutations causing strong expression of the OLE1p-PHO5 fusion gene under repression conditions (presence of oleic acid), were isolated. Results of Northern analysis of OLE1 as well as OLE1p-PHO5 transcripts in nfo mutants suggested that these mutations occurred in genes encoding global repressors. We also demonstrated that TUP1 and SSN6 gene products are required for full repression of OLE1 gene expression, by showing that either tup1 or ssn6 mutations greatly increase the level of the OLE1 transcript."}, "year": 1997, "reftypes": [{"display_name": "Journal Article"}], "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1016/s0014-5793(97)00846-6"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/9280286"}]}, {"id": 592637, "display_name": "Ando S, et al. (1996)", "link": "/reference/S000058429", "citation": "Ando S, et al. (1996) Phylogenetic relationships of species of the genus Saccharomyces Meyen ex Reess deduced from partial base sequences of 18S and 26S ribosomal RNAs (saccharomycetaceae). Biosci Biotechnol Biochem 60(7):1070-5", "pubmed_id": 8782400, "abstract": {"text": "In order to clarify the phylogenetic relationships among the yeast species classified in the genus Saccharomyces, partial base sequences of 18S and 26S ribosomal RNAs were determined for ten selected strains. The regions determined correspond to positions 1451 through 1618 of the 18S rRNA and positions 493 through 622 and 1611 through 1835 of the 26S rRNA in S. cerevisiae. Analyses of these partial base sequences suggested that the genus Saccharomyces is phylogenetically heterogeneous. Saccharomyces servazzii and S. unisporus showed identical or very similar sequences in all the three regions, and their phylogenetic distance from S. cerevisiae was large enough to introduce a genus independent of Saccharomyces. Saccharomyces kluyveri is also distant from all the other Saccharomyces species examined, and is likely to deserve a new genus. Estimated phylogenetic relationships between Saccharomyces and other genera characterized by the Q-6 system, such as species of Zygosaccharomyces. Torulaspora, Kluyveromyces, Arxiozyma, Pachytichospora, Nadsonia. Hanseniaspora, Kloeckeraspora, and Saccharomycodes, are also discussed."}, "year": 1996, "reftypes": [{"display_name": "Comparative Study"}, {"display_name": "Journal Article"}], "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1271/bbb.60.1070"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/8782400"}]}, {"id": 598184, "display_name": "Yoshino M, et al. (1992)", "link": "/reference/S000056500", "citation": "Yoshino M, et al. (1992) Inhibition by aluminum ion of NAD- and NADP-dependent isocitrate dehydrogenases from yeast. Int J Biochem 24(10):1615-8", "pubmed_id": 1397488, "abstract": {"text": "1. NADP-dependent isocitrate dehydrogenase from yeast was potently inhibited by aluminum ion competitively with respect to the substrate isocitrate, and noncompetitively with the other substrate NADP. Ki value was determined to be 0.43 microM. 2. Aluminum ion acted as only a weak allosteric inhibitor of yeast NAD-dependent isocitrate dehydrogenase toward isocitrate, and as a noncompetitive inhibitor toward NAD. 3. Inhibition by aluminum ion of NADP- and NAD-isocitrate dehydrogenases can reduce the aerobic energy production in yeast, and may contribute to the biological toxicity of aluminum in ecosystems and human life."}, "year": 1992, "reftypes": [{"display_name": "Journal Article"}], "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1016/0020-711x(92)90178-4"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/1397488"}]}]};