Streptothricin F, an inhibitor of protein synthesis with miscoding activity.

Haupt, Ina; Hübener, Rainer; Thrum, H.

doi:10.7164/antibiotics.31.1137

Cited by 38 publications

(31 citation statements)

References 10 publications

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“…Exposure to oleate allows entry of Sytox into cells either because oleate directly influences processes at the plasma membrane to allow dye to enter the cell or because oleate kills the cells by some other means after which the dead cells become permeable to Sytox. To distinguish between these two possibilities, yeast were killed by poisoning with clonNAT, a drug that is known to kill by mistranslation (Haupt et al 1978). Although ,5% of either Pex 1 or pex6D cells were viable after 2 hr of clonNAT treatment, there was no increase in Sytoxpositive cells of either the Pex 1 ( Figure 8A) or the pex6D (data not shown) strain even after 4 hr of clonNAT treatment.…”

Section: Resultsmentioning

confidence: 88%

The Sensitivity of Yeast Mutants to Oleic Acid Implicates the Peroxisome and Other Processes in Membrane Function

et al. 2007

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The peroxisome, sole site of b-oxidation in Saccharomyces cerevisiae, is known to be required for optimal growth in the presence of fatty acid. Screening of the haploid yeast deletion collection identified 130 genes, 23 encoding peroxisomal proteins, necessary for normal growth on oleic acid. Oleate slightly enhances growth of wild-type yeast and inhibits growth of all strains identified by the screen. Nonperoxisomal processes, among them chromatin modification by H2AZ, Pol II mediator function, and cell-wall-associated activities, also prevent oleate toxicity. The most oleate-inhibited strains lack Sap190, a putative adaptor for the PP2A-type protein phosphatase Sit4 (which is also required for normal growth on oleate) and Ilm1, a protein of unknown function. Palmitoleate, the other main unsaturated fatty acid of Saccharomyces, fails to inhibit growth of the sap190D, sit4D, and ilm1D strains. Data that suggest that oleate inhibition of the growth of a peroxisomal mutant is due to an increase in plasma membrane porosity are presented. We propose that yeast deficient in peroxisomal and other functions are sensitive to oleate perhaps because of an inability to effectively control the fatty acid composition of membrane phospholipids.

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Section: Resultsmentioning

confidence: 88%

The Sensitivity of Yeast Mutants to Oleic Acid Implicates the Peroxisome and Other Processes in Membrane Function

et al. 2007

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“…Similarly, we have noted a very modest elevation in spontaneous mutation rate in both the U. maydis rad51-1 and rec2-1 mutants, easily quantified by measuring forward mutation to drug resistance using any one of a number of metabolic inhibitors or antibiotics. We utilized the drug, nourseothricin, a streptothricin-related polyamine antibiotic that interferes with translation via direct binding to ribosomes (Haupt et al, 1978;Cundliffe, 1989). Measuring spontaneous mutation by forward resistance to this compound is convenient as backgrounds are clean and identification of resistant mutants is unambiguous.…”

Section: Rec2-197 Has Elevated Spontaneous Mutator Activitymentioning

confidence: 99%

Disruptions of the Ustilago maydis REC2 gene identify a protein domain important in directing recombinational repair of DNA

Kojic

Thompson

Holloman

2001

Molecular Microbiology

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The REC2 gene of Ustilago maydis encodes a homologue of the Escherichia coli RecA protein and was first identified in a screen for UV‐sensitive mutants. The original isolate, rec2‐1, was found to be deficient in repair of DNA damage, genetic recombination and meiosis. We report here that the rec2‐197 allele, which was constructed by gene disruption, retains some biological activity and is partially dominant with respect to REC2. The basis for the residual activity is probably as a result of expression of a diffusible product from the rec2‐197 allele that augments or interferes with REC2 functions. This product appears to be a polypeptide expressed from a remnant of the 5′ end of the open reading frame that was not removed in creating the gene disruption. The mutator activity and disturbed meiosis of rec2‐197 suggest that the Rec2 protein functions in a process that avoids spontaneous mutation and insures faithful meiotic chromosome segregation. A prediction based on the phenotype of rec2‐197 is that Rec2 protein interacts with one or more other proteins in directing these functions. To identify interacting proteins we performed a yeast two‐hybrid screen and found Rad51 as a candidate. Rec2‐197 and Rad51 appear to interact to a similar degree.

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“…Beide Antibioticagruppen sind typische Heinmstoffe der Translokation der Proteinsynthese und induzieren ein falsches Ablesen der genetischen Informat'ion (HAUPT et al 1978, 1980, CABAK-4S et ctl. 1978a, b, ~~I S U M I et al 1978.…”

Section: Diskzcssionunclassified

Isolierung von Streptothricin‐resistenten Mutanten aus Escherichia coli K12, Stamm A19

Seidel

Haupt

1982

J of Basic Microbiology

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Isolierung von Streptothricin-resistentenMutanten aus Escherichia coli K12, Stamm A19 L. 8EIDEL und INA HAUPT (Eingegangen urn 26. 4.1981) Mutants with various levels of resistance t o streptothricin were isolated from Escherichia coli K12, strain A19 after mutagenesis with N-methyl-N-nitro-N-nitroso-guanidine and ethylmethane-sulfonate. Nourseothricin, a mixture of streptothricin F and D was the selection agent. Spontaneous resistant mutants could not be found. The streptothricin-resistant mutant E. coli A19 Stcr 2/2/1 shows cross-resistance to some of the aminoglycoside antibiotics investigated, but no cross-resistance t o chloramphenicol and chlortetracyclin. These results indicate similar mechanisms of action of streptothricin and aminoglycoside antibiotics.

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Streptothricin F, an inhibitor of protein synthesis with miscoding activity.

Cited by 38 publications

References 10 publications

The Sensitivity of Yeast Mutants to Oleic Acid Implicates the Peroxisome and Other Processes in Membrane Function

The Sensitivity of Yeast Mutants to Oleic Acid Implicates the Peroxisome and Other Processes in Membrane Function

Disruptions of the Ustilago maydis REC2 gene identify a protein domain important in directing recombinational repair of DNA

Isolierung von Streptothricin‐resistenten Mutanten aus Escherichia coli K12, Stamm A19

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