Academic literature on the topic 'Saccharomyces cerevisiae Eukaryotes'
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Journal articles on the topic "Saccharomyces cerevisiae Eukaryotes"
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.
Full textMarshall, 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.
Full textde 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.
Full textKane, 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.
Full textWalters, 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.
Full textHarris, 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.
Full textHall, 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.
Full textNeff, 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.
Full textGalcheva-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.
Full textPeccarelli, 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.
Full textDissertations / Theses on the topic "Saccharomyces cerevisiae Eukaryotes"
Haider, Mustafa M. "The intracellular sorting of vacuolar proteins in the yeast Saccharomyces cerevisiae." Thesis, Durham University, 1989. http://etheses.dur.ac.uk/6495/.
Full textKubicek, 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.
Full textPost-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
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.
Full textPereira, 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/.
Full textThe 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.
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.
Full textKipling, 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.
Full textBalyan, 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.
Full textFan-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.
Full textJackson, Stephen Philip. "Cloning and characterisation of the RNA8 gene of Saccharomyces cerevisiae." Thesis, University of Edinburgh, 1987. http://hdl.handle.net/1842/15100.
Full textKallmeyer, 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.
Full textBooks on the topic "Saccharomyces cerevisiae Eukaryotes"
Vasilescu, S. Structure function and intracellular localisation of the eukaryotic initiation factor eIF4E in theyeast Saccharomyces cerevisiae. Manchester: UMIST, 1996.
Find full textInstability of simple sequence DNA in Saccharomyces cervisiae. 1992.
Find full textBook chapters on the topic "Saccharomyces cerevisiae Eukaryotes"
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.
Full textNg, 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.
Full textTye, 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.
Full textToh-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.
Full textIcho, 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.
Full textThuriaux, 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.
Full textMerkl, 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.
Full textDannenmaier, 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.
Full textBraun, 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.
Full textPulitzer, 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.
Full textConference papers on the topic "Saccharomyces cerevisiae Eukaryotes"
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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