Academic literature on the topic 'Yeast Trp1'

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Journal articles on the topic "Yeast Trp1"

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Roth, S. Y., A. Dean, and R. T. Simpson. "Yeast alpha 2 repressor positions nucleosomes in TRP1/ARS1 chromatin." Molecular and Cellular Biology 10, no. 5 (May 1990): 2247–60. http://dx.doi.org/10.1128/mcb.10.5.2247-2260.1990.

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The yeast alpha 2 repressor suppresses expression of a-mating-type-specific genes in haploid alpha and diploid a/alpha cell types. We inserted the alpha 2-binding site into the multicopy TRP1/ARS1 yeast plasmid and examined the effects of alpha 2 on the chromatin structure of the derivative plasmids in alpha cells, and a/alpha cells. Whereas no effect on nucleosome position was observed in a cells, nucleosomes were precisely and stably positioned over sequences flanking the alpha 2 operator in alpha and a/alpha cells. In addition, when the alpha 2 operator was located upstream of the TRP1 gene, an extended array of positioned nucleosomes was formed in alpha cells and a/alpha cells, with formation of a nucleosome not present in a cells, and TRP1 mRNA production was substantially reduced. These data indicate that alpha 2 causes a positioning of nucleosomes over sequences proximal to its operator in TRP1/ARS1 chromatin and suggest that changes in chromatin structure may be related to alpha 2 repression of cell-type-specific genes.
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Roth, S. Y., A. Dean, and R. T. Simpson. "Yeast alpha 2 repressor positions nucleosomes in TRP1/ARS1 chromatin." Molecular and Cellular Biology 10, no. 5 (May 1990): 2247–60. http://dx.doi.org/10.1128/mcb.10.5.2247.

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The yeast alpha 2 repressor suppresses expression of a-mating-type-specific genes in haploid alpha and diploid a/alpha cell types. We inserted the alpha 2-binding site into the multicopy TRP1/ARS1 yeast plasmid and examined the effects of alpha 2 on the chromatin structure of the derivative plasmids in alpha cells, and a/alpha cells. Whereas no effect on nucleosome position was observed in a cells, nucleosomes were precisely and stably positioned over sequences flanking the alpha 2 operator in alpha and a/alpha cells. In addition, when the alpha 2 operator was located upstream of the TRP1 gene, an extended array of positioned nucleosomes was formed in alpha cells and a/alpha cells, with formation of a nucleosome not present in a cells, and TRP1 mRNA production was substantially reduced. These data indicate that alpha 2 causes a positioning of nucleosomes over sequences proximal to its operator in TRP1/ARS1 chromatin and suggest that changes in chromatin structure may be related to alpha 2 repression of cell-type-specific genes.
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Sikorski, R. S., and P. Hieter. "A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae." Genetics 122, no. 1 (May 1, 1989): 19–27. http://dx.doi.org/10.1093/genetics/122.1.19.

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Abstract A series of yeast shuttle vectors and host strains has been created to allow more efficient manipulation of DNA in Saccharomyces cerevisiae. Transplacement vectors were constructed and used to derive yeast strains containing nonreverting his3, trp1, leu2 and ura3 mutations. A set of YCp and YIp vectors (pRS series) was then made based on the backbone of the multipurpose plasmid pBLUESCRIPT. These pRS vectors are all uniform in structure and differ only in the yeast selectable marker gene used (HIS3, TRP1, LEU2 and URA3). They possess all of the attributes of pBLUESCRIPT and several yeast-specific features as well. Using a pRS vector, one can perform most standard DNA manipulations in the same plasmid that is introduced into yeast.
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Heitman, J., A. Koller, J. Kunz, R. Henriquez, A. Schmidt, N. R. Movva, and M. N. Hall. "The immunosuppressant FK506 inhibits amino acid import in Saccharomyces cerevisiae." Molecular and Cellular Biology 13, no. 8 (August 1993): 5010–19. http://dx.doi.org/10.1128/mcb.13.8.5010-5019.1993.

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The immunosuppressants cyclosporin A, FK506, and rapamycin inhibit growth of unicellular eukaryotic microorganisms and also block activation of T lymphocytes from multicellular eukaryotes. In vitro, these compounds bind and inhibit two different types of peptidyl-prolyl cis-trans isomerases. Cyclosporin A binds cyclophilins, whereas FK506 and rapamycin bind FK506-binding proteins (FKBPs). Cyclophilins and FKBPs are ubiquitous, abundant, and targeted to multiple cellular compartments, and they may fold proteins in vivo. Previously, a 12-kDa cytoplasmic FKBP was shown to be only one of at least two FK506-sensitive targets in the yeast Saccharomyces cerevisiae. We find that a second FK506-sensitive target is required for amino acid import. Amino acid-auxotrophic yeast strains (trp1 his4 leu2) are FK506 sensitive, whereas prototrophic strains (TRP1 his4 leu2, trp1 HIS4 leu2, and trp1 his4 LEU2) are FK506 resistant. Amino acids added exogenously to the growth medium mitigate FK506 toxicity. FK506 induces GCN4 expression, which is normally induced by amino acid starvation. FK506 inhibits transport of tryptophan, histidine, and leucine into yeast cells. Lastly, several genes encoding proteins involved in amino acid import or biosynthesis confer FK506 resistance. These findings demonstrate that FK506 inhibits amino acid import in yeast cells, most likely by inhibiting amino acid transporters. Amino acid transporters are integral membrane proteins which import extracellular amino acids and constitute a protein family sharing 30 to 35% identity, including eight invariant prolines. Thus, the second FK506-sensitive target in yeast cells may be a proline isomerase that plays a role in folding amino acid transporters during transit through the secretory pathway.
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Heitman, J., A. Koller, J. Kunz, R. Henriquez, A. Schmidt, N. R. Movva, and M. N. Hall. "The immunosuppressant FK506 inhibits amino acid import in Saccharomyces cerevisiae." Molecular and Cellular Biology 13, no. 8 (August 1993): 5010–19. http://dx.doi.org/10.1128/mcb.13.8.5010.

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The immunosuppressants cyclosporin A, FK506, and rapamycin inhibit growth of unicellular eukaryotic microorganisms and also block activation of T lymphocytes from multicellular eukaryotes. In vitro, these compounds bind and inhibit two different types of peptidyl-prolyl cis-trans isomerases. Cyclosporin A binds cyclophilins, whereas FK506 and rapamycin bind FK506-binding proteins (FKBPs). Cyclophilins and FKBPs are ubiquitous, abundant, and targeted to multiple cellular compartments, and they may fold proteins in vivo. Previously, a 12-kDa cytoplasmic FKBP was shown to be only one of at least two FK506-sensitive targets in the yeast Saccharomyces cerevisiae. We find that a second FK506-sensitive target is required for amino acid import. Amino acid-auxotrophic yeast strains (trp1 his4 leu2) are FK506 sensitive, whereas prototrophic strains (TRP1 his4 leu2, trp1 HIS4 leu2, and trp1 his4 LEU2) are FK506 resistant. Amino acids added exogenously to the growth medium mitigate FK506 toxicity. FK506 induces GCN4 expression, which is normally induced by amino acid starvation. FK506 inhibits transport of tryptophan, histidine, and leucine into yeast cells. Lastly, several genes encoding proteins involved in amino acid import or biosynthesis confer FK506 resistance. These findings demonstrate that FK506 inhibits amino acid import in yeast cells, most likely by inhibiting amino acid transporters. Amino acid transporters are integral membrane proteins which import extracellular amino acids and constitute a protein family sharing 30 to 35% identity, including eight invariant prolines. Thus, the second FK506-sensitive target in yeast cells may be a proline isomerase that plays a role in folding amino acid transporters during transit through the secretory pathway.
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Thorsness, P. E., and T. D. Fox. "Nuclear mutations in Saccharomyces cerevisiae that affect the escape of DNA from mitochondria to the nucleus." Genetics 134, no. 1 (May 1, 1993): 21–28. http://dx.doi.org/10.1093/genetics/134.1.21.

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Abstract We have inserted a yeast nuclear DNA fragment bearing the TRP1 gene and its associated origin of DNA replication, ARS1, into the functional mitochondrial chromosome of a strain carrying a chromosomal trp1 deletion. TRP1 was not phenotypically expressed within the organelle. However, this Trp- strain readily gave rise to respiratory competent Trp+ clones that contained the TRP1/ARS1 fragment, associated with portions of mitochondrial DNA (mtDNA), replicating in their nuclei. Thus the Trp+ clones arose as a result of DNA escaping from mitochondria and migrating to the nucleus. We have isolated 21 nuclear mutants in which the rate of mtDNA escape is increased by screening for increased rates of papillation to Trp+. All 21 mutations were recessive and fell into six complementation groups, termed YME1-YME6. In addition to increasing the rate of mtDNA escape, yme1 mutations also caused a heat-sensitive respiratory deficient phenotype at 37 degrees and a cold-sensitive growth defect on complete glucose medium at 14 degrees. While the other yme mutations had no detectable growth phenotypes, synergistic interactions were observed in two double mutant combinations: a yme1, yme2 double mutant failed to respire at 30 degrees and a yme4, yme6 double mutant failed to respire at all temperatures tested. None of the respiratory defects were caused by loss of functional mtDNA. These findings suggest that yme1, yme2, yme4 and yme6 mutations alter mitochondrial functions and thereby lead to an increased rate of DNA escape from the organelle.
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Rodríguez-Vargas, Sonia, Alicia Sánchez-García, Jose Manuel Martínez-Rivas, Jose Antonio Prieto, and Francisca Randez-Gil. "Fluidization of Membrane Lipids Enhances the Tolerance of Saccharomyces cerevisiae to Freezing and Salt Stress." Applied and Environmental Microbiology 73, no. 1 (October 27, 2006): 110–16. http://dx.doi.org/10.1128/aem.01360-06.

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ABSTRACT Unsaturated fatty acids play an essential role in the biophysical characteristics of cell membranes and determine the proper function of membrane-attached proteins. Thus, the ability of cells to alter the degree of unsaturation in their membranes is an important factor in cellular acclimatization to environmental conditions. Many eukaryotic organisms can synthesize dienoic fatty acids, but Saccharomyces cerevisiae can introduce only a single double bond at the Δ9 position. We expressed two sunflower (Helianthus annuus) oleate Δ12 desaturases encoded by FAD2-1 and FAD2-3 in yeast cells of the wild-type W303-1A strain (trp1) and analyzed their effects on growth and stress tolerance. Production of the heterologous desaturases increased the content of dienoic fatty acids, especially 18:2Δ9,12, the unsaturation index, and the fluidity of the yeast membrane. The total fatty acid content remained constant, and the level of monounsaturated fatty acids decreased. Growth at 15°C was reduced in the FAD2 strains, probably due to tryptophan auxotrophy, since the trp1 (TRP1) transformants that produced the sunflower desaturases grew as well as the control strain did. Our results suggest that changes in the fluidity of the lipid bilayer affect tryptophan uptake and/or the correct targeting of tryptophan transporters. The expression of the sunflower desaturases, in either Trp+ or Trp− strains, increased NaCl tolerance. Production of dienoic fatty acids increased the tolerance to freezing of wild-type cells preincubated at 30°C or 15°C. Thus, membrane fluidity is an essential determinant of stress resistance in S. cerevisiae, and engineering of membrane lipids has the potential to be a useful tool of increasing the tolerance to freezing in industrial strains.
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Braus, G. H., K. Luger, G. Paravicini, T. Schmidheini, K. Kirschner, and R. Hütter. "The role of the TRP1 gene in yeast tryptophan biosynthesis." Journal of Biological Chemistry 263, no. 16 (June 1988): 7868–75. http://dx.doi.org/10.1016/s0021-9258(18)68578-3.

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Manfredi, J. P., C. Klein, J. J. Herrero, D. R. Byrd, J. Trueheart, W. T. Wiesler, D. M. Fowlkes, and J. R. Broach. "Yeast alpha mating factor structure-activity relationship derived from genetically selected peptide agonists and antagonists of Ste2p." Molecular and Cellular Biology 16, no. 9 (September 1996): 4700–4709. http://dx.doi.org/10.1128/mcb.16.9.4700.

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alpha-Factor, a 13-amino-acid pheromone secreted by haploid alpha cells of Saccharomyces cerevisiae, binds to Ste2p, a seven-transmembrane, G-protein-coupled receptor present on haploid alpha cells, to activate a signal transduction pathway required for conjugation and mating. To determine the structural requirements for alpha-factor activity, we developed a genetic screen to identify from random and semirandom libraries novel peptides that function as agonists or antagonists of Ste2p. The selection scheme was based on autocrine strains constructed to secrete random peptides and respond by growth to those that were either agonists or antagonists of Ste2p. Analysis of a number of peptides obtained by this selection procedure indicates that Trp1, Trp3, Pro8, and Gly9 are important for agonist activity specifically. His2, Leu4, Leu6, Pro10, a hydrophobic residue 12, and an aromatic residue 13 are important for both agonist and antagonist activity. Our results also show that activation of Ste2p can be achieved with novel, unanticipated combinations of amino acids. Finally, the results suggest the utility of this selection scheme for identifying novel ligands for mammalian G-protein-coupled receptors heterologously expressed in S. cerevisiae.
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Long, C. M., C. M. Brajkovich, and J. F. Scott. "Alternative model for chromatin organization of the Saccharomyces cerevisiae chromosomal DNA plasmid TRP1 RI circle (YARp1)." Molecular and Cellular Biology 5, no. 11 (November 1985): 3124–30. http://dx.doi.org/10.1128/mcb.5.11.3124-3130.1985.

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TRP1 RI circle (now designated YARp1, yeast acentric ring plasmid 1) is a 1,453-base-pair artificial plasmid composed exclusively of Saccharomyces cerevisiae chromosomal DNA. It contains both the TRP1 gene and ARS1 (a DNA sequence that permits extrachromosomal maintenance of recombinant plasmids). This high-copy-number, relatively stable plasmid was shown to be organized into nucleosomes comparable to typical yeast chromatin, containing a possible maximum of nine nucleosomes per circle. Therefore, YARp1 can be used to examine the structure of chromatin of both a chromosomally derived replicator and a functional gene. By mapping regions of micrococcal nuclease cleavage in chromatin versus purified DNA, we located the positions of protected regions on the circle with reference to six unique restriction sites. Measurements made on patterns of early digestion products indicated that a region of approximately 300 base pairs in the vicinity of ARS1 was strongly resistant to micrococcal nuclease. The remainder of the plasmid appeared to be associated with five positioned nucleosomes and two nonnucleosomal, partially protected regions on the bulk of the molecules. After similar extents of digestion, naked DNA did not exhibit an equivalent pattern, although some hypersensitive cleavage sites matched sites found in the chromatin. These results are consistent with the interpretation that the protected domains are aligned with respect to a specific site or sites on the small circular chromatin.
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Dissertations / Theses on the topic "Yeast Trp1"

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Krappmann, Sven Kurt. "Biosynthesis of Aromatic Amino Acids in Yeast and Aspergillus." Doctoral thesis, [S.l. : s.n.], 2000. http://hdl.handle.net/11858/00-1735-0000-000D-F20C-1.

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Qian, Feng. "Mouse TRP4 and its associated proteins /." 2000. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&res_dat=xri:pqdiss&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&rft_dat=xri:pqdiss:9965042.

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Lin, Junyu. "A yeast model for ion-channel ER export : how Yvclp, a yeast TRP channel homolog, is exported out of the ER /." 2002. http://www.library.wisc.edu/databases/connect/dissertations.html.

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Kulesza, Caroline Ann. "Adenovirus E1A requires the yeast SAGA histone acetyltransferase complex and associates with SAGA component Tra1 in vivo /." 2001. http://wwwlib.umi.com/dissertations/fullcit/3003890.

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Books on the topic "Yeast Trp1"

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McNeel, Douglas Gordon. Identification and characterization of TRF1: A DNA-binding protein in a yeast linear DNA plasmid system. 1992.

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Book chapters on the topic "Yeast Trp1"

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Rezwan, Mandana, Nicolas Lentze, Lukas Baumann, and Daniel Auerbach. "Application of the Split-Protein Sensor Trp1 to Protein Interaction Discovery in the Yeast Saccharomyces cerevisiae." In Methods in Molecular Biology, 245–58. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-455-1_14.

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Kaleta, Marta, and Christopher Palmer. "TRP Channels in Yeast." In Transient Receptor Potential Channels, 315–21. Dordrecht: Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-94-007-0265-3_17.

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Moiseenkova-Bell, Vera, and Theodore G. Wensel. "Functional and Structural Studies of TRP Channels Heterologously Expressed in Budding Yeast." In Transient Receptor Potential Channels, 25–40. Dordrecht: Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-94-007-0265-3_2.

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Koerner, T. J., John E. Hill, Alan M. Myers, and Alexander Tzagoloff. "[33] High-expression vectors with multiple cloning sites for construction of trpE fusion genes: pATH vectors." In Guide to Yeast Genetics and Molecular Biology, 477–90. Elsevier, 1991. http://dx.doi.org/10.1016/0076-6879(91)94036-c.

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Hrycyna, Christine A., Stephanie J. Wait, Peter S. Backlund, and Susan Michaelis. "[21] Yeast STE 14 methyltransferase, expressed as TrpE-STE 14 fusion protein in Escherichia coli, for in Vitro Carboxylmethylation of prenylated polypeptides." In Methods in Enzymology, 251–66. Elsevier, 1995. http://dx.doi.org/10.1016/0076-6879(95)50077-4.

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