Relevant bibliographies by topics / Saccharomyces cerevisiae Eukaryotes

Academic literature on the topic 'Saccharomyces cerevisiae Eukaryotes'

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Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Saccharomyces cerevisiae Eukaryotes"

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Tamm, Tiina, Ivan Kisly, and Jaanus Remme. "Functional Interactions of Ribosomal Intersubunit Bridges in Saccharomyces cerevisiae." Genetics 213, no. 4 (October 24, 2019): 1329–39. http://dx.doi.org/10.1534/genetics.119.302777.

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Ribosomes of Archaea and Eukarya share higher homology with each other than with bacterial ribosomes. For example, there is a set of 35 r-proteins that are specific only for archaeal and eukaryotic ribosomes. Three of these proteins—eL19, eL24, and eL41—participate in interactions between ribosomal subunits. The eukaryote-specific extensions of r-proteins eL19 and eL24 form two intersubunit bridges eB12 and eB13, which are present only in eukaryotic ribosomes. The third r-protein, eL41, forms bridge eB14. Notably, eL41 is found in all eukaryotes but only in some Archaea. It has been shown that bridges eB12 and eB13 are needed for efficient translation, while r-protein eL41 plays a minor role in ribosome function. Here, the functional interactions between intersubunit bridges were studied using budding yeast strains lacking different combinations of the abovementioned bridges/proteins. The growth phenotypes, levels of in vivo translation, ribosome–polysome profiles, and in vitro association of ribosomal subunits were analyzed. The results show a genetic interaction between r-protein eL41 and the eB12 bridge-forming region of eL19, and between r-proteins eL41 and eL24. It was possible to construct viable yeast strains with Archaea-like ribosomes lacking two or three eukaryote-specific bridges. These strains display slow growth and a poor translation phenotype. In addition, bridges eB12 and eB13 appear to cooperate during ribosome subunit association. These results indicate that nonessential structural elements of r-proteins become highly important in the context of disturbed subunit interactions. Therefore, eukaryote-specific bridges may contribute to the evolutionary success of eukaryotic translation machinery.
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Marshall, Alexandra N., Jaeil Han, Minseon Kim, and Ambro van Hoof. "Conservation of mRNA quality control factor Ski7 and its diversification through changes in alternative splicing and gene duplication." Proceedings of the National Academy of Sciences 115, no. 29 (July 2, 2018): E6808—E6816. http://dx.doi.org/10.1073/pnas.1801997115.

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Eukaryotes maintain fidelity of gene expression by preferential degradation of aberrant mRNAs that arise by errors in RNA processing reactions. In Saccharomyces cerevisiae, Ski7 plays an important role in this mRNA quality control by mediating mRNA degradation by the RNA exosome. Ski7 was initially thought to be restricted to Saccharomyces cerevisiae and close relatives because the SKI7 gene and its paralog HBS1 arose by whole genome duplication (WGD) in a recent ancestor. We have recently shown that the preduplication gene was alternatively spliced and that Ski7 function predates WGD. Here, we use transcriptome analysis of diverse eukaryotes to show that diverse eukaryotes use alternative splicing of SKI7/HBS1 to encode two proteins. Although alternative splicing affects the same intrinsically disordered region of the protein, the pattern of splice site usage varies. This alternative splicing event arose in an early eukaryote that is a common ancestor of plants, animals, and fungi. Remarkably, through changes in alternative splicing and gene duplication, the Ski7 protein has diversified such that different species express one of four distinct Ski7-like proteins. We also show experimentally that the Saccharomyces cerevisiae SKI7 gene has undergone multiple changes that are incompatible with the Hbs1 function and may also have undergone additional changes to optimize mRNA quality control. The combination of transcriptome analysis in diverse eukaryotes and genetic analysis in yeast clarifies the mechanism by which a Ski7-like protein is expressed across eukaryotes and provides a unique view of changes in alternative splicing patterns of one gene over long evolutionary time.
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de Silva, D. M., C. C. Askwith, and J. Kaplan. "Molecular mechanisms of iron uptake in eukaryotes." Physiological Reviews 76, no. 1 (January 1, 1996): 31–47. http://dx.doi.org/10.1152/physrev.1996.76.1.31.

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Iron serves essential functions in both prokaryotes and eukaryotes, and cells have highly specialized mechanisms for acquiring and handling this metal. The primary mechanism by which the concentration of iron in biologic systems is controlled is through the regulation of iron uptake. Although the role of transferrin in mammalian iron homeostasis has been well characterized, the study of genetic disorders of iron metabolism has revealed other, transferrin-independent, mechanisms by which cells can acquire iron. In an attempt to understand how eukaryotic systems take up this essential element, investigators have begun studying the simple eukaryote Saccharomyces cerevisiae. Several genes have been identified and cloned that act in concert to allow iron acquisition from the environment. Some of these genes appear to have functional homologues in human systems. This review focuses on the recent developments in understanding eukaryotic iron uptake with an emphasis on the genetic and molecular characterization of these systems in both cultured mammalian cells and S. cerevisiae. An unexpected connection between iron and copper homeostasis has been revealed by recent genetic studies, which confirm biologic observations made several decades ago.
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Kane, Patricia M. "The Where, When, and How of Organelle Acidification by the Yeast Vacuolar H+-ATPase." Microbiology and Molecular Biology Reviews 70, no. 1 (March 2006): 177–91. http://dx.doi.org/10.1128/mmbr.70.1.177-191.2006.

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SUMMARY All eukaryotic cells contain multiple acidic organelles, and V-ATPases are central players in organelle acidification. Not only is the structure of V-ATPases highly conserved among eukaryotes, but there are also many regulatory mechanisms that are similar between fungi and higher eukaryotes. These mechanisms allow cells both to regulate the pHs of different compartments and to respond to changing extracellular conditions. The Saccharomyces cerevisiae V-ATPase has emerged as an important model for V-ATPase structure and function in all eukaryotic cells. This review discusses current knowledge of the structure, function, and regulation of the V-ATPase in S. cerevisiae and also examines the relationship between biosynthesis and transport of V-ATPase and compartment-specific regulation of acidification.
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Walters, Robert W., Tyler Matheny, Laura S. Mizoue, Bhalchandra S. Rao, Denise Muhlrad, and Roy Parker. "Identification of NAD+ capped mRNAs in Saccharomyces cerevisiae." Proceedings of the National Academy of Sciences 114, no. 3 (December 28, 2016): 480–85. http://dx.doi.org/10.1073/pnas.1619369114.

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RNAs besides tRNA and rRNA contain chemical modifications, including the recently described 5′ nicotinamide-adenine dinucleotide (NAD+) RNA in bacteria. Whether 5′ NAD-RNA exists in eukaryotes remains unknown. We demonstrate that 5′ NAD-RNA is found on subsets of nuclear and mitochondrial encoded mRNAs in Saccharomyces cerevisiae. NAD-mRNA appears to be produced cotranscriptionally because NAD-RNA is also found on pre-mRNAs, and only on mitochondrial transcripts that are not 5′ end processed. These results define an additional 5′ RNA cap structure in eukaryotes and raise the possibility that this 5′ NAD+ cap could modulate RNA stability and translation on specific subclasses of mRNAs.
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Harris, C. L., and C. J. Kolanko. "Aminoacyl-tRNA synthetase complex in Saccharomyces cerevisiae." Biochemical Journal 309, no. 1 (July 1, 1995): 321–24. http://dx.doi.org/10.1042/bj3090321.

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The size distribution of aminoacyl-tRNA synthetase activity was investigated in cell extracts prepared from Saccharomyces cerevisiae. Bio-Gel A-5M chromatography of 105,000 g supernatants separated isoleucyl-tRNA synthetase activity into three peaks, with apparent molecular masses (Da) of about 100,000, 350,000 and 10(6) or greater. Similar results were obtained with synthetases specific for glutamic acid, serine and tyrosine. Sucrose-density-gradient centrifugation of yeast supernatants also provided evidence for the existence of synthetase complexes. These data provide the first evidence for the existence of a high-molecular-mass aminoacyl-tRNA synthetase complex in yeast, perhaps similar to those reported in higher eukaryotes.
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Hall, Charles, Sophie Brachat, and Fred S. Dietrich. "Contribution of Horizontal Gene Transfer to the Evolution of Saccharomyces cerevisiae." Eukaryotic Cell 4, no. 6 (June 2005): 1102–15. http://dx.doi.org/10.1128/ec.4.6.1102-1115.2005.

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ABSTRACT The genomes of the hemiascomycetes Saccharomyces cerevisiae and Ashbya gossypii have been completely sequenced, allowing a comparative analysis of these two genomes, which reveals that a small number of genes appear to have entered these genomes as a result of horizontal gene transfer from bacterial sources. One potential case of horizontal gene transfer in A. gossypii and 10 potential cases in S. cerevisiae were identified, of which two were investigated further. One gene, encoding the enzyme dihydroorotate dehydrogenase (DHOD), is potentially a case of horizontal gene transfer, as shown by sequencing of this gene from additional bacterial and fungal species to generate sufficient data to construct a well-supported phylogeny. The DHOD-encoding gene found in S. cerevisiae, URA1 (YKL216W), appears to have entered the Saccharomycetaceae after the divergence of the S. cerevisiae lineage from the Candida albicans lineage and possibly since the divergence from the A. gossypii lineage. This gene appears to have come from the Lactobacillales, and following its acquisition the endogenous eukaryotic DHOD gene was lost. It was also shown that the bacterially derived horizontally transferred DHOD is required for anaerobic synthesis of uracil in S. cerevisiae. The other gene discussed in detail is BDS1, an aryl- and alkyl-sulfatase gene of bacterial origin that we have shown allows utilization of sulfate from several organic sources. Among the eukaryotes, this gene is found in S. cerevisiae and Saccharomyces bayanus and appears to derive from the alpha-proteobacteria.
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Neff, Carrie L., and Alan B. Sachs. "Eukaryotic Translation Initiation Factors 4G and 4A from Saccharomyces cerevisiae Interact Physically and Functionally." Molecular and Cellular Biology 19, no. 8 (August 1, 1999): 5557–64. http://dx.doi.org/10.1128/mcb.19.8.5557.

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ABSTRACT The initiation of translation in eukaryotes requires several multisubunit complexes, including eukaryotic translation initiation factor 4F (eIF4F). In higher eukaryotes eIF4F is composed of the cap binding protein eIF4E, the adapter protein eIF4G, and the RNA-stimulated ATPase eIF4A. The association of eIF4A withSaccharomyces cerevisiae eIF4F has not yet been demonstrated, and therefore the degree to which eIF4A’s conserved function relies upon this association has remained unclear. Here we report an interaction between yeast eIF4G and eIF4A. Specifically, we found that the growth arrest phenotype associated with three temperature-sensitive alleles of yeast eIF4G2 was suppressed by excess eIF4A and that this suppression was allele specific. In addition, in vitro translation extracts derived from an eIF4G2 mutant strain could be heat inactivated, and this inactivation could be reversed upon the addition of recombinant eIF4A. Finally, in vitro binding between yeast eIF4G and eIF4A was demonstrated, as was diminished binding between mutant eIF4G2 proteins and eIF4A. In total, these data indicate that yeast eIF4G and eIF4A physically associate and that this association performs an essential function.
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Galcheva-Gargova, Zoya, and Lubomira Stateva. "Immunological identification of two lamina-like proteins in Saccharomyces cerevisiae." Bioscience Reports 8, no. 3 (June 1, 1988): 287–91. http://dx.doi.org/10.1007/bf01115046.

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Proteins from Saccharomyces cerevisiae were tested for their crossreactivity with antibodies raised against nuclear lamina proteins of Ehrlich Ascites Tumour cells. The results of the immunoblotting experiments and ELISA suggest the existence of at least two proteins (65 and 59 kDa) which are immunologically related to the nuclear lamina proteins of higher eukaryotes.
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Peccarelli, Megan, and Bessie W. Kebaara. "Regulation of Natural mRNAs by the Nonsense-Mediated mRNA Decay Pathway." Eukaryotic Cell 13, no. 9 (July 18, 2014): 1126–35. http://dx.doi.org/10.1128/ec.00090-14.

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ABSTRACT The nonsense-mediated mRNA decay (NMD) pathway is a specialized mRNA degradation pathway that degrades select mRNAs. This pathway is conserved in all eukaryotes examined so far, and it triggers the degradation of mRNAs that prematurely terminate translation. Originally identified as a pathway that degrades mRNAs with premature termination codons as a result of errors during transcription, splicing, or damage to the mRNA, NMD is now also recognized as a pathway that degrades some natural mRNAs. The degradation of natural mRNAs by NMD has been identified in multiple eukaryotes, including Saccharomyces cerevisiae , Drosophila melanogaster , Arabidopsis thaliana , and humans. S. cerevisiae is used extensively as a model to study natural mRNA regulation by NMD. Inactivation of the NMD pathway in S. cerevisiae affects approximately 10% of the transcriptome. Similar percentages of natural mRNAs in the D. melanogaster and human transcriptomes are also sensitive to the pathway, indicating that NMD is important for the regulation of gene expression in multiple organisms. NMD can either directly or indirectly regulate the decay rate of natural mRNAs. Direct NMD targets possess NMD-inducing features. This minireview focuses on the regulation of natural mRNAs by the NMD pathway, as well as the features demonstrated to target these mRNAs for decay by the pathway in S. cerevisiae . We also compare NMD-targeting features identified in S. cerevisiae with known NMD-targeting features in other eukaryotic organisms.
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Dissertations / Theses on the topic "Saccharomyces cerevisiae Eukaryotes"

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Haider, Mustafa M. "The intracellular sorting of vacuolar proteins in the yeast Saccharomyces cerevisiae." Thesis, Durham University, 1989. http://etheses.dur.ac.uk/6495/.

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The mechanism of protein sorting to the vacuole in yeast was studied both in vitro and in vivo. A series of experiments were performed to reconstitute transport of carboxypeptidase Y (CPY) from Golgi vesicles to vacuoles. In order to investigate this process, microsomes were purified from sec, pep4-3 mutant strains that accumulate inactive proCPY in the Golgi when incubated at the nonpermissive temperature. These were mixed with purified vacuoles isolated from a mutant lacking CPY activity, but containing active proteinases A and B. Transported proCPY is maturated by these proteinases to active form. Experiments indicate that maturation of CPY is due to the correct transport of proCPY from microsomes to vacuoles because:- Firstly, the reaction is temperature sensitive, requires ATP and is stimulated by the addition of soluble factors (S100). Secondly, the addition of proteinase A and B inhibitors to the reaction mixtures has a negligible effect on the maturation process. Thirdly, disrupting the membranes by the addition of Triton X-100 before addition of the proteinase inhibitors, inhibited the maturation of proCPY. Fourthly, the majority of CPY activity was observed in the sedimented fraction of the reaction mixtures rather than supernatant fractions. Lastly, analysis with western blot shows a clear band of mature CPY only in the sedimented fraction of the reaction mixtures with ATP. This in vitro system will be invaluable in investigating the molecular events of vacuolar biogenesis. For in vivo sorting of proteins to the vacuole, a series of experiments were performed that involved the genetic fusion of the CPY promoter and prepro-sequence of CPY to the bacterial Gus (β-glucuronidase) reporter gene. The Gus gene was expressed in yeast with high efficiency and the results of sub-cellular fractionation indicated that the Gus product was distributed in all cell components. Using a centromeric vector gave similar results but with a lower efficiency of Gus expression. Removal of 90bp from Gus, including Gus initiation codon does not completely inhibit Gus expression either in bacteria or in yeast. Fusion of the shortened Gus with the CPY prepro-fragment and expression in yeast led to the correct sorting of the CPY-Gus hybrid protein to the vacuole. This CPY-Gus fusion is potentially useful in the genetic analysis of mutations defective in vacuolar protein sorting.
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Kubicek, Charles E. 1981. "Identifying targets and function of the ubiquitin related modifier Urm1 in Saccharomyces cerevisiae." Thesis, University of Oregon, 2009. http://hdl.handle.net/1794/10310.

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xi, 81 p. : ill. A print copy of this thesis is available through the UO Libraries. Search the library catalog for the location and call number.
Post-translational modification of proteins is an important cellular method of controlling various aspects of protein activity, including protein-protein interactions, half- life, and transport. An important class of post-translational modifications involves the ubiquitin family of proteins. In these modifications, a small protein, such as ubiquitin, is conjugated to a target protein through an isopeptide bond. Conjugation by a ubiquitin family member acts as a signal to regulate the activity, function, or stability of the target protein. Urm1, a ubiquitin-like protein conserved throughout all eukaryotes, was initially identified in S. cerevisiae. Loss of Urm1 leads to the disruption of a variety of cellular processes, including oxidative stress response, filamentous growth, and temperature sensitivity. This body of work comprises efforts to identify novel targets of Urm1, the mechanism by which Urm1 is attached to target proteins, and the physiological consequences of such conjugation. To gain understanding of the function and mechanism of Urm1 conjugation, the only known conjugate of Urm1, the peroxiredoxin reductase Ahp1, was examined in an effort to identify the site of modification on Ahp1 and to evaluate the physiological consequences of urmylation of Ahp1. I then completed a series of screens--a synthetic lethal screen, a two-hybrid screen, and a protein over-expression screen--to identify novel Urm1 conjugates and cellular functions dependent on Urm1. Of particular interest were genes identified in the synthetic lethal screen, namely PTC1, which encodes a protein phosphatase, and a set of genes encoding the Elongator complex, which functions in transcriptional elongation and tRNA modification. During this time period, other groups showed that thiolation of tRNAs depends on Urm1. Thus, Urm1 does not function only in protein conjugation, but also as a sulfur carrier in the thiolation of tRNA. Interestingly, I identified Elp2, a component of the Elongator complex, as a new Urm1-conjugate. Because Elp2 is also required for tRNA modification, perhaps Urm1 plays more than one role in tRNA modification. Loss of tRNA modification may disrupt many cellular functions and could explain the variety of urm1 mutant phenotypes. I have determined that all known Urm1 dependent processes are also associated with tRNA modification.
Committee in charge: Karen Guillemin, Chairperson, Biology; George Sprague, Advisor, Biology; Alice Barkan, Member, Biology; Kenneth Prehoda, Member, Chemistry; Tom Stevens, Outside Member, Chemistry
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Bartish, Galyna. "Elongation factor 2 : a key component of the translation machinery in eukaryotes : properties of yeast elongation factor 2 studied in vivo /." Stockholm : Wenner-Gren Institute for Experimental Biology, Stockholm university, 2008. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-7733.

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Pereira, Dirce Maria Carraro. "Regulação transcricional por glicose do promotor do gene que codifica celobiohidrolase I de Trichoderma reesei em Saccharomyces cerevisiae." Universidade de São Paulo, 1998. http://www.teses.usp.br/teses/disponiveis/46/46131/tde-27112014-152253/.

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O sistema celulolítico do fungo filamentoso Trichoderma reesei é induzido transcricionalmente em pelo menos 1000 vezes pelo crescimento do fungo na presença de celulose e fortemente reprimido por glicose. Usando a abordagem de deleção no promotor, determinou-se que a região localizada entre -241 e -72 bp, em relação ao TATA box, denominada UARcb1, é responsável pela transcrição estimulada por celulose da enzima celobiohidrolase I (cbhl). Neste trabalho mostramos que essa região controla a transcrição de um gene repórter, sofrendo repressão por glicose, em Saccharomyces cerevisiae, um microrganismo que não possui os genes necessários para a utilização de celulose. A transcrição mediada por UARcbl, que é controlada por glicose, requer o produto do gene SNFl, uma proteína quinase, e dois repressores: SSN6 e TUP1, cujos papéis no controle de genes reprimidos por glicose, na levedura, são bem estabelecidos. Nossos resultados indicam um mecanismo conservado de controle por glicose em microrganismos eucarióticos.
The cellulotic system of the filamentous fungus Trichoderma reesei is transcriptionally induced 1000 -fold in presence of cellulose and is strongly repressed by glucose. Using the promoter deletion approach, the upstream activating region (UARcbl) responsible for cellulose-stimulated transcription of the major member of the cellulase system, cellobiohydrolase I, was localized between -241 and -72 relative to the TATA box. In this work we show that this region controls transcription and mediates glucose repression of a reporter gene in Saccharomyces cerevisiae, a unicellular microorganism that lacks the genes required for the utilization of cellulose. Glucose-controlled transcription mediated by the UARcbl requires the product of SNF1 gene, a protein kinase, and two repressors SSN6 and TUP1, which are well estalished in controlling glucose-represible yeast genes. Our results indicate a conserved mechanism of glucose control in eukariotic microorganisms.
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Chommy, Hélène. "Fidélité de la traduction chez les eucaryotes. De la molécule au génome." Phd thesis, Université Paris Sud - Paris XI, 2012. http://tel.archives-ouvertes.fr/tel-00749760.

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Ce travail porte sur l'étude de la fidélité de la traduction chez les eucaryotes d'un point de vue mécanistique et génomique. Au cours de ma thèse j'ai développé trois approches :Le premier projet porte sur l'étude du rôle du facteur de l'élongation eEF2 dans le maintien du cadre de lecture. La stratégie associe une mutagénèse aléatoire du gène EFT2 à un criblage phénotypique, elle permet d'isoler des mutants capables d'augmenter ou diminuer l'efficacité de recodage d'une séquence de décalage du cadre de lecture en -1.Le second projet décrit la mise au point d'un système de traduction en molécule unique qui permet d'étudier le ribosome eucaryote. La traduction est initiée grâce à l'IRES CrPV qui a pour caractéristique d'être totalement indépendante des facteurs d'initiation et de l'ARNt initiateur. L'élongation de la traduction est détectée grâce au départ d'un oligonucléotide fluorescent qui est décroché par l'activité hélicase du ribosome. Les résultats de ces expériences constituent une preuve de principe démontrant que l'étude de la traduction eucaryote en molécule unique est possible.Le troisième projet est une étude de génomique comparative qui permet de rechercher des événements de recodage ainsi que d'autres événements non-conventionnels de la traduction dans le génome de la levure Saccharomyces cerevisiae. L'approche est basée sur une recherche d'organisations génomiques conservées au sein de 19 génomes de levures. Les gènes candidats sont testés in vivo grâce à un vecteur double rapporteur. Cette étude a permis de mettre en évidence le gène VOA1 qui a été ensuite caractérisé plus en détails.
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Kipling, D. G. "Studies on replication origins in Saccharomyces cerevisiae." Thesis, University of Oxford, 1989. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.253151.

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Balyan, Prachi. "Complex genetic interactions in the model eukaryote, Saccharomyces cerevisiae." Thesis, University of Cambridge, 2015. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.709165.

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Fan-Minogue, Hua. "Understanding the molecular mechanism of eukaryotic translation termination functional analysis of ribosomal RNA and eukaryotic release factor one /." Thesis, Birmingham, Ala. : University of Alabama at Birmingham, 2007. https://www.mhsl.uab.edu/dt/2009r/fan-minogue.pdf.

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Jackson, Stephen Philip. "Cloning and characterisation of the RNA8 gene of Saccharomyces cerevisiae." Thesis, University of Edinburgh, 1987. http://hdl.handle.net/1842/15100.

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Kallmeyer, Adam K. "Regulatory mechanisms of eukaryotic translation termination." Thesis, Birmingham, Ala. : University of Alabama at Birmingham, 2007. https://www.mhsl.uab.edu/dt/2009r/kallmeyer.pdf.

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Books on the topic "Saccharomyces cerevisiae Eukaryotes"

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Vasilescu, S. Structure function and intracellular localisation of the eukaryotic initiation factor eIF4E in theyeast Saccharomyces cerevisiae. Manchester: UMIST, 1996.

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Instability of simple sequence DNA in Saccharomyces cervisiae. 1992.

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Book chapters on the topic "Saccharomyces cerevisiae Eukaryotes"

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Wickner, Reed B., Tsutomu Fujimura, and Rosa Esteban. "Overview of Double-Stranded RNA Replication In Saccharomyces Cerevisiae." In Extrachromosomal Elements in Lower Eukaryotes, 149–63. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5251-8_12.

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Ng, Ray, Janice Ness, and John Carbon. "Structural Studies on Centromeres in the Yeast Saccharomyces Cerevisiae." In Extrachromosomal Elements in Lower Eukaryotes, 479–92. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5251-8_36.

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Tye, Bik-Kwoon, Pratima Sinha, Richard Surosky, Susan Gibson, Gregory Maine, and Shlomo Eisenberg. "Host Factors in Nuclear Plasmid Maintenance in Saccharomyces Cerevisiae." In Extrachromosomal Elements in Lower Eukaryotes, 499–510. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5251-8_38.

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Toh-e, A., and Y. Sahashi. "Structure and Function of the PET18 Locus of Saccharomyces Cerevisiae." In Extrachromosomal Elements in Lower Eukaryotes, 189–202. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5251-8_15.

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Icho, Tateo, Hyun-Sook Lee, Steve S. Sommer, and Reed B. Wickner. "Molecular Characterization of Chromosomal Genes Affecting Double-Stranded RNA Replication in Saccharomyces Cerevisiae." In Extrachromosomal Elements in Lower Eukaryotes, 165–71. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5251-8_13.

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Thuriaux, Pierre, Carl Mann, Jean-Marie Buhler, Isabelle Treich, Rosmarie Gudenus, Sylvie Mariotte, Michel Riva, and André Sentenac. "Gene Cloning and Mutant Isolation of Subunits of RNA Polymerases in the Yeast Saccharomyces Cerevisiae." In Extrachromosomal Elements in Lower Eukaryotes, 519–31. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5251-8_40.

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Merkl, Philipp E., Christopher Schächner, Michael Pilsl, Katrin Schwank, Catharina Schmid, Gernot Längst, Philipp Milkereit, Joachim Griesenbeck, and Herbert Tschochner. "Specialization of RNA Polymerase I in Comparison to Other Nuclear RNA Polymerases of Saccharomyces cerevisiae." In Ribosome Biogenesis, 63–70. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2501-9_4.

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AbstractIn archaea and bacteria the major classes of RNAs are synthesized by one DNA-dependent RNA polymerase (RNAP). In contrast, most eukaryotes have three highly specialized RNAPs to transcribe the nuclear genome. RNAP I synthesizes almost exclusively ribosomal (r)RNA, RNAP II synthesizes mRNA as well as many noncoding RNAs involved in RNA processing or RNA silencing pathways and RNAP III synthesizes mainly tRNA and 5S rRNA. This review discusses functional differences of the three nuclear core RNAPs in the yeast S. cerevisiae with a particular focus on RNAP I transcription of nucleolar ribosomal (r)DNA chromatin.
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Dannenmaier, Stefan, Silke Oeljeklaus, and Bettina Warscheid. "2nSILAC for Quantitative of Prototrophic Baker’s Yeast." In Methods in Molecular Biology, 253–70. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1024-4_18.

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AbstractStable isotope labeling by amino acids in cell culture (SILAC) combined with high-resolution mass spectrometry is a quantitative strategy for the comparative analysis of (sub)proteomes. It is based on the metabolicincorporation of stable isotope-coded amino acids during growth of cells or organisms. Here, complete labeling of proteins with the amino acid(s) selected for incorporation needs to be guaranteed to enable accurate quantification on a proteomic scale. Wild-type strains of baker’s yeast (Saccharomyces cerevisiae), which is a widely accepted and well-studied eukaryotic model organism, are generally able to synthesize all amino acids on their own (i.e., prototrophic). To render them amenable to SILAC, auxotrophies are introduced by genetic manipulations. We addressed this limitation by developing a generic strategy for complete “native” labeling of prototrophic S. cerevisiae with isotope-coded arginine and lysine, referred to as “2nSILAC”. It allows for directly using and screening several genome-wide yeast mutant collections that are easily accessible to the scientific community for functional proteomic studies but are based on prototrophic variants of S. cerevisiae.
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Braun, Christina, Robert Knüppel, Jorge Perez-Fernandez, and Sébastien Ferreira-Cerca. "Non-radioactive In Vivo Labeling of RNA with 4-Thiouracil." In Ribosome Biogenesis, 199–213. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2501-9_12.

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Abstract:
AbstractRNA molecules and their expression dynamics play essential roles in the establishment of complex cellular phenotypes and/or in the rapid cellular adaption to environmental changes. Accordingly, analyzing RNA expression remains an important step to understand the molecular basis controlling the formation of cellular phenotypes, cellular homeostasis or disease progression. Steady-state RNA levels in the cells are controlled by the sum of highly dynamic molecular processes contributing to RNA expression and can be classified in transcription, maturation and degradation. The main goal of analyzing RNA dynamics is to disentangle the individual contribution of these molecular processes to the life cycle of a given RNA under different physiological conditions. In the recent years, the use of nonradioactive nucleotide/nucleoside analogs and improved chemistry, in combination with time-dependent and high-throughput analysis, have greatly expanded our understanding of RNA metabolism across various cell types, organisms, and growth conditions.In this chapter, we describe a step-by-step protocol allowing pulse labeling of RNA with the nonradioactive nucleotide analog, 4-thiouracil, in the eukaryotic model organism Saccharomyces cerevisiae and the model archaeon Haloferax volcanii.
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10

Pulitzer, John F., and Alessandra Pollice. "Gene regulatory circuits in Saccharomyces cerevisiae as a tool for the identification of heterologous eukaryotic regulatory elements." In Molecular Biology and its Application to Medical Mycology, 75–83. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-84625-0_10.

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Conference papers on the topic "Saccharomyces cerevisiae Eukaryotes"

1

Altuntas, Volkan, and Murat Gok. "The stability and fragility of biological networks: Eukaryotic model organism Saccharomyces cerevisiae." In 2017 International Conference on Computer Science and Engineering (UBMK). IEEE, 2017. http://dx.doi.org/10.1109/ubmk.2017.8093575.

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