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  • 1
    Electronic Resource
    Electronic Resource
    Human tryptophanyl-tRNA synthetase can efficiently complement the Saccharoymces cerevisiae homologue, Wrs1P (2002)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 216 (2002), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Aminoacyl-tRNA synthetases corresponding to each of the 20 amino acids are essential proteins for nearly all cells. The tryptophan-specific enzyme in the cytoplasm of Saccharomyces cerevisiae (ScWRS) is a 49-kDa protein encoded by the WRS1 gene and required for survival. The human enzyme (HsWRS) is a 54-kDa protein with 46% sequence identity to ScWRS. HsWRS has a kinase domain in the N-terminal region and a serine phosphorylation site near the C-terminus not present in the yeast enzyme. To determine if the gene encoding the human protein could functionally complement the WRS1 gene, HsWRS cDNA was cloned in the expression vectors pVT100U and pYES then transformed into a diploid yeast where one copy of WRS1 had been replaced with a G418R gene. Tetrads derived from these transformants were dissected and spores germinated on media selecting for the presence of the plasmids. Haploid colonies were then tested for resistance to G418. G418R cells were unable to grow in the presence of 5-fluoroorotic acid, indicating their dependence on the plasmids for viability. Polymerase chain reaction analysis of these cells confirmed the presence of the HsWRS gene and the absence of WRS1. Growth rates of cells expressing HsWRS are essentially identical to the parent. This demonstrates that the human enzyme can function in yeast and effectively replace the ScWRS protein in spite of the presence of two unique functions and a 〉50% overall difference in amino acid sequence.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2002.tb11423.x
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  • 2
    Electronic Resource
    Electronic Resource
    Mechanisms of mitochondrial DNA escape to the nucleus in the yeast Saccharomyces cerevisiae (1999)
    Springer
    Current genetics 36 (1999), S. 183-194 
    Details
    ISSN: 1432-0983
    Keywords: Key words Mitochondrial DNA escape ; Mitochondria ; Yeast ; Plasmids
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The transfer of organelle nucleic acid to the nucleus has been observed in both plants and animals. Using a unique assay to monitor mitochondrial DNA escape to the nucleus in the yeast Saccharomyces cerevisiae, we previously showed that mutations in several nuclear genes, collectively called yme mutants, cause a high rate of mitochondrial DNA escape to the nucleus. Here we demonstrate that mtDNA escape occurs via an intracellular mechanism that is dependent on the composition of the growth medium and the genetic state of the mitochondrial genome, and is independent of an RNA intermediate. Isolation of several unique second-site suppressors of the high rate of mitochondrial DNA-escape phenotype of yme mutants suggests that there are multiple independent pathways by which this nucleic acid transfer occurs. We also demonstrate that the presence of centromeric plasmids in the nucleus can reduce the perceived rate of DNA escape from the mitochondria. We propose that mitochondrial DNA-escape events are manifested as unstable nuclear plasmids that can interact with centromeric plasmids resulting in a decrease in the number of observed events.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050489
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  • 3
    Electronic Resource
    Electronic Resource
    AFG2, an essential gene in yeast, encodes a new member of the Sec18p, Pas1p, Cdc48p, TBP-1 family of putative ATPases (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 1267-1271 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A gene from Saccharomyces cerevisiae was sequenced that encodes a protein with homology to a family of putative ATPases. These homologous proteins include the yeast cell division cycle protein Cdc48p and its mammalian homologues VCP and p97; Sec18p and its mammalian homologue NSF, proteins necessary for fusion of transport vesicles to target membranes in the secretory pathway; Pas1p, a protein necessary for peroxisome biosynthesis in yeast; Yme1p, a yeast mitochondrial protein that influences the rate of DNA escape from mitochondria; and TBP-1, MSS1 and Sug1p, proteins that interact with transcription factors. This newly sequenced gene, named AFG2 for ATPase family gene, is located on chromosome XII 5′ to the SLP1/VPS33 open reading reading frame and encodes an essential protein of 780 amino acids that is most homologous to Cdc48p.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091114
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