A Trichodermin‐Resistant Mutant of <i>Saccharomyces cerevisiae</i> with an Abnormal Distribution of Native Ribosomal Subunits

Carter, Christopher; Cannon, Michael; Jiménez, Antonio Moreno

doi:10.1111/j.1432-1033.1980.tb04638.x

Cited by 22 publications

(8 citation statements)

References 30 publications

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“…It is likely that DON would be produced in the cells juxtaposed the hyphal tip [148]. Since DON may inhibit protein synthesis [148,149] inhibition of host enzyme synthesis following fungal presence/toxin production would facilitate fungal colonisation of the host tissue. Plants resistant to DON should therefore demonstrate increased resistance to spread following colonisation [36].…”

Section: Prevention Of Fungal Spreadmentioning

confidence: 99%

The phytotoxicity ofFusarium metabolites: An update since 1989

McLean

1996

Mycopathologia

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The present article summarises the published phytotoxic effects of severalFusarium metabolites (mycotoxins, phytotoxins, antibiotics and pigments) since 1989. The phytotoxicity of many of the commonly isolated metabolites cannot be disputed, but their role in pathogenesis ofFusarium-induced plant diseases is uncertain. Plant species/varieties differ in their susceptibililty resistance to these toxinsin vitro, as well as toFusarium pathogens under field conditions. Such variations in plant response may reflect resistance mechanisms that operate at several levels, including an initial ability to prevent fungal invasion; prevention of fungal spread and toxin tolerance or degradation. Little is known about the mode of action of most of these metabolites on either animal or plant cells. Several novelFusarium metabolites have been isolated in the past few years. Many are toxic to animals and cell lines, but assessment of their phytotoxicity has largely been neglected. Since many plant pathogenic Fusaria produce a plethora of metabolites, the additive or synergistic actions of toxins in combination must be considered in plant pathology.

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Section: Prevention Of Fungal Spreadmentioning

confidence: 99%

The phytotoxicity ofFusarium metabolites: An update since 1989

McLean

1996

Mycopathologia

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“…Sodium azide (final concentration 1 mM) was added and, after a further 15-min incubation, the cells were slow-cooled to 10°C and harvested as described elsewhere (Carter et al, 1980). Cells were broken by two passages through an ice-cold French pressure cell at 1.33 MPa; high-salt-washed 80s ribosomes and supernatant fractions were prepared essentially as described in AdouttePanvier and Davies (1984).…”

Section: Polyphenylalanine Synthesis In Yeast Cell-free Systemsmentioning

confidence: 99%

Natural cycloheximide resistance in yeast

Dehoux¹,

Davies²,

Cannon

1993

European Journal of Biochemistry

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The yest Kluyveromyces lactis is resistant to high concentrations (1 mg/ml) of the antibiotic cycloheximide. Using in vitro translation studies it was confirmed that this extreme resistance is a property of ribosomes. The resistance determinant from K. lactis was cloned into Saccharomyces cerevisiae. Nucleotide sequence analysis of the determinant demonstrated that resistance was conferred by the K. Lactis ribosomal protein L41. K. lactis was shown to contain only one copy of the gene that encodes this protein and the gene was located to chromosome III. In contrast, S. cerevisiae was found to contain multiple copies of the gene for the corresponding ribosomal protein L41 which mapped to two of the three chromosomes V, XIV and VIII. Since the cycloheximide‐resistance gene of K. lactis causes essentially complete protection against inhibition by the drug, it is likely to be particularly useful as a selective marker in eukaryotic gene transfer studies.

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“…Proteins associated with the ribosomal precursor RNPs are also thought to be modified (for a review, see reference 18). A number of yeast mutants affected in rRNA processing have been identified (1,2,9,17,20,31,41,(48)(49)(50). Among these mutants, however, only a single temperature-sensitive (ts) lethal mutant, ts351, was found to be defective specifically in the conversion of 27S pre-rRNA to mature 25S and 5.8S rRNAs (1).…”

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confidence: 99%

RRP1, a Saccharomyces cerevisiae gene affecting rRNA processing and production of mature ribosomal subunits

Fabian¹,

Hopper²

1987

J Bacteriol

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The Saccharomyces cerevisiae mutant ts351 had been shown to affect processing of 27S pre-rRNA to mature 25S and 5.8S rRNAs (C. Andrew, A. K. Hopper, and B. D. Hall, Mol. Gen. Genet. 144:29-37, 1976). We showed that this strain contains two mutations leading to temperature-sensitive lethality. The rRNA-processing defect, however, is a result of only one of the two mutations. We designated the lesion responsible for the rRNA-processing defect rrp) and showed that it is located on the right arm of chromosome IV either allelic to or tightly linked to mak2l. This rip) lesion also results in hypersensitivity to aminoglycoside antibiotics and a reduced 25S/18S rRNA ratio at semipermissive temperatures. We cloned the RRPI gene and provide evidence that it encodes a moderately abundant mRNA which is in lower abundance and larger than most mRNAs encoding ribosomal proteins.In many respects, rRNA processing in the yeast Saccharormyces cerevisiae is similar to what has been observed in higher eucaryotes (51). The primary pre-rRNA (35S) transcript is not normally processed before transcription termination (33). Before association of proteins with the primary pre-rRNA transcript, the latter is extensively modified (for a review, see reference 38). These modifications are, for the most part, at positions destined to become mature rRNAs (27). Undermethylation of the pre-rRNAs leads to poor processing (5, 53). The general pathway of the processing steps for yeast rRNAs is as follows. The primary 35S pre-rRNA is cleaved to produce 20S and 27S pre-rRNAs. These pre-rRNAs are then processed to produce, respectively, the mature 185 rRNA and the 25S and 5.8S rRNAs (19,43,45). The enzymes catalyzing these reactions are not well defined.Normally, processing of the rRNAs requires assembly of the 35S pre-rRNA into a ribonucleoprotein particle (RNP) (44; for reviews, see references 18, 19, and 51). The prerRNP particle that contains the 35S pre-rRNA (the 90S RNP) is converted to 43S and 66S RNPs containing the 20S pre-rRNA and associated proteins. The 43S RNP moves from the nucleus to the cytoplasm, Where the 20S pre-rRNA is processed to the 18S mature rRNA and the 43S RNP is converted to the mature 40S ribosomal subunit. Conversion of the 66S RNP (21S pre-rRNA) to the mature 60S ribosonial subunit containing the 25S and 5.8S rRNAs is a nuclear rather than a cytoplasmic event (44, 46; for a review, see reference 18).Present on the precursor ribosomal 90S of these modifications is not known (for reviews, see references 38 and 51). Proteins associated with the ribosomal precursor RNPs are also thought to be modified (for a review, see reference 18). A number of yeast mutants affected in rRNA processing have been identified (1,2,9,17,20,31,41,(48)(49)(50). Among these mutants, however, only a single temperature-sensitive (ts) lethal mutant, ts351, was found to be defective specifically in the conversion of 27S pre-rRNA to mature 25S and 5.8S rRNAs (1). Gorenstein and Warner (16) further demonstrated that the 27S pre-rRNA was relatively unstab...

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A Trichodermin‐Resistant Mutant of Saccharomyces cerevisiae with an Abnormal Distribution of Native Ribosomal Subunits

Cited by 22 publications

References 30 publications

The phytotoxicity ofFusarium metabolites: An update since 1989

The phytotoxicity ofFusarium metabolites: An update since 1989

Natural cycloheximide resistance in yeast

RRP1, a Saccharomyces cerevisiae gene affecting rRNA processing and production of mature ribosomal subunits

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