Vitamin Deficiencies in Yeasts

Burkholder, Paul R.

doi:10.1002/j.1537-2197.1943.tb14749.x

Cited by 92 publications

(20 citation statements)

References 11 publications

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“…All strains of S. pombe were grown in rich medium, YES [3% glucose, 0.5% yeast extract (Difco Laboratories) and 100 mg/l each of adenine, uracil, leucine, and histidine], or in synthetic medium, Burkholder medium without thiamine (Burkholder 1943, Andoh et al 1995. The general genetic methods that were used for S. pombe have been described previously (Gutz et al 1974;Moreno et al 1991).…”

Section: Strains Media and Genetic Methodsmentioning

confidence: 99%

Phosphoinositide-specific phospholipase C forms a complex with 14-3-3 proteins and is involved in expression of UV resistance in fission yeast

Andoh

Kato²,

Matsui

et al. 1998

Mol Gen Genet

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The fission yeast plc1+ gene encodes phosphoinositide-specific phospholipase C. The two- hybrid interaction assay with plexA-plc1+ as a bait revealed that Plc1p interacted with the 14-3-3 proteins Rad24p and Rad25p. Formation of a complex containing Plc1p and Rad24p in vivo was confirmed by an immunological method. As predicted from the fact that rad24 null mutant cells are hypersensitive to UV irradiation, plc1 null mutant cells were almost as sensitive to UV irradiation as rad24 null mutant cells. In addition, deletion of rad24 in the plc1 null mutant cells did not enhance the UV sensitivity, indicating that plc1+ and rad24+ belong to the same epistasis group with respect to UV sensitivity. Whereas Rad24p has been reported to be involved in the DNA damage checkpoint pathway, the delay to mitosis after UV irradiation was not defective either in rad24 null mutant cells or in plcl null mutant cells in our analysis. Thus, Plc1p is responsible for resistance to UV irradiation, but not for the DNA damage checkpoint pathway, in cooperation with 14-3-3 proteins.

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Section: Strains Media and Genetic Methodsmentioning

confidence: 99%

Phosphoinositide-specific phospholipase C forms a complex with 14-3-3 proteins and is involved in expression of UV resistance in fission yeast

Andoh

Kato²,

Matsui

et al. 1998

Mol Gen Genet

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“…SC/glucose + FOA medium contained 1 mg of 5-fluoroorotic acid (5-FOA) per ml (6). The low-phosphate SC-MetCys medium was prepared according the formula of Burkholder (8) Tyl transposition assays. Strain YH49 was use iments involving a-factor and nocodazole treat cells were first grown on SC-Ura/glucose plates f 30°C.…”

Section: Methodsmentioning

confidence: 99%

Inhibition of Ty1 transposition by mating pheromones in Saccharomyces cerevisiae.

Boeke

1991

Mol. Cell. Biol.

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The Tyl elements in the yeast Saccharomyces cerevisiae are a family of retrotransposons which transpose via a process similar to that of retroviral replication. We report here that the Tyl transposition process can be blocked posttranscriptionally by treatment of cells with mating pheromones. When haploid yeast cells are treated with appropriate mating pheromones, the transposition frequency of a marked Tyl element driven by the GAL] promoter is greatly diminished. Tyl viruslike particles (VLPs), the putative intermediates for transposition, can be isolated from mating pheromone-treated cells. These VLPs accumulate to normal levels but are aberrant in that they produce very few reverse transcripts of Tyl RNA both in vivo and in vitro and contain subnormal amounts of p90-TYB and related proteins. In addition, a TYA phosphoprotein product accumulates in treated cells, and some species of TYB proteins have decreased stability. We also show that decreased transposition in mating pheromone-treated cells is not a consequence of simply blocking cell division, since Tyl transposes at a nearly normal rate in yeast cells arrested in G2 by the drug nocodazole.Transposable elements carry out the breakage of host DNA and the insertion of new DNA. Clearly, the frequency of these potentially deleterious reactions must be stringently regulated. In Escherichia coli, the well-studied transposon TnJO is regulated transcriptionally, translationally, and at the level of the transposition reaction itself (21). In yeast cells, the transposition of Tyl elements is known to be controlled transcriptionally both by the MAT locus and by several SPT loci, yet examples of posttranscriptional regulatory mechanisms are few (3).Tyl elements, a family of retrotransposons in the yeast Saccharomyces cerevisiae, are approximately 6 kb long and consist of a central coding region flanked by long terminal repeats. The two open reading frames in Tyl include TYA, which corresponds to retroviral gag, and TYB, which corresponds to pol (3). Previous studies indicate that Tyl elements transpose via a mechanism analogous to that of retroviral replication and that the functions and relationships of Tyl-encoded proteins are also very similar to those of retroviral proteins (1,5,26,36). Specifically, TYB proteins are initially synthesized as a fusion product of the TYA and TYB open reading frames (p190-TYA/TYB). Both TYB and TYA precursor proteins are processed by a Tyl-encoded protease to smaller products (Fig. 1); this processing is essential for transposition (36). It has been shown that TYA proteins are phosphorylated, although it is not known whether the phosphorylation plays any role in transposition (23). Viruslike particles (VLPs) have been isolated from yeast cells in which Tyl RNAs are overexpressed (19,24). VLPs are apparently direct intermediates for transposition; they are capable of reverse transcribing Tyl RNA and integrating Tyl cDNA, two key steps in the life cycle of Tyl elements (15,16,19,24).

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“…YEPD medium contained 1% (w/v) Yeast Extract (Difco), 2% (w/v) peptone (Difco) and 2% (w/v) glucose. For induction of APase, KH2P04 was replaced by equimolar (1 1 mM) KCl in Burkholder medium (Burkholder, 1943). Glucose was replaced by galactose for efficient incorporation of [,H]mannose.…”

Section: Methodsmentioning

confidence: 99%