Sodium azide-induced mutagenesis in Saccharomyces cerevisiae

Šilhánková, L.; Smiovská, V.; Velemínský, J.

doi:10.1016/0027-5107(79)90125-8

Cited by 17 publications

(3 citation statements)

References 12 publications

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“…50 μ L (∼10 million cells) were plated on YPD plates containing 6% ethanol and either UV irradiated at a wavelength of 302 nm for 10 sec, with a survival rate of ∼10%, or simply incubated at 30°. An independent set of cultures was also treated with sodium azide following the protocol outlined by Silhánková et al (1979) . Colonies that grew after 4 days at 30° were isolated under non-selective conditions and their growth reanalyzed on YPD containing 6% ethanol.…”

Section: Methodsmentioning

confidence: 99%

The Pseudokinase Domain of Saccharomyces cerevisiae Tra1 Is Required for Nuclear Localization and Incorporation into the SAGA and NuA4 Complexes

Berg

Genereaux

Karagiannis

et al. 2018

G3 Genes|Genomes|Genetics

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Tra1 is an essential component of the SAGA/SLIK and NuA4 complexes in S. cerevisiae, recruiting these co-activator complexes to specific promoters. As a PIKK family member, Tra1 is characterized by a C-terminal phosphoinositide 3-kinase (PI3K) domain. Unlike other PIKK family members (e.g., Tor1, Tor2, Mec1, Tel1), Tra1 has no demonstrable kinase activity. We identified three conserved arginine residues in Tra1 that reside proximal or within the cleft between the N- and C-terminal subdomains of the PI3K domain. To establish a function for Tra1’s PI3K domain and specifically the cleft region, we characterized a tra1 allele where these three arginine residues are mutated to glutamine. The half-life of the Tra1Q3 protein is reduced but its steady state level is maintained at near wild-type levels by a transcriptional feedback mechanism. The tra1Q3 allele results in slow growth under stress and alters the expression of genes also regulated by other components of the SAGA complex. Tra1Q3 is less efficiently transported to the nucleus than the wild-type protein. Likely related to this, Tra1Q3 associates poorly with SAGA/SLIK and NuA4. The ratio of Spt7SLIK to Spt7SAGA increases in the tra1Q3 strain and truncated forms of Spt20 become apparent upon isolation of SAGA/SLIK. Intragenic suppressor mutations of tra1Q3 map to the cleft region further emphasizing its importance. We propose that the PI3K domain of Tra1 is directly or indirectly important for incorporating Tra1 into SAGA and NuA4 and thus the biosynthesis and/or stability of the intact complexes.

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Section: Methodsmentioning

confidence: 99%

The Pseudokinase Domain of Saccharomyces cerevisiae Tra1 Is Required for Nuclear Localization and Incorporation into the SAGA and NuA4 Complexes

Berg

Genereaux

Karagiannis

et al. 2018

G3 Genes|Genomes|Genetics

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“…Sodium azide is mutagenic in several plant systems (32,37,38,46) mammalian cells in culture (47) bacteria (31) and yeast (49). It can also be metabolized by plants into a mutagen (41).…”

Section: In Vivo Plant Activationmentioning

confidence: 99%

Plant Dependent Mutation Assays

Gentile

Plewa

1982

Genetic Toxicology

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“…Sodium azide has been used to study various biological processes such as the fermentative ability of yeast grown under different oxygen conditions [ 10 ]. Interestingly, it has also been used as a weak mutagen in yeast protoplasts [ 11 ]. It increases thermo-tolerance of glucose-grown yeast [ 12 ] and is routinely used in studies of mRNA translation control since sodium azide treatment leads to general translation repression [ 13 ].…”

Section: Introductionmentioning

confidence: 99%

Elucidation of the RNA-granule inducing sodium azide stress response through transcriptome analysis

Poornima

Rajyaguru

2020

Genomics

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Sodium azide is a commonly used cytochrome oxidase inhibitor that leads to translation repression and RNA granule assembly. The global changes in mRNA abundance in response to this stressor are unknown. RGG-motif proteins Scd6 and Sbp1 are translation-repressors and decapping-activators that localize to and affect the assembly of RNA granules in response to sodium azide stress. Transcriptome-wide effects of these proteins remain unknown. To address this, we have sequenced transcriptome of the: a) wild type strain under unstressed and sodium azide stress, b) Δscd6 and Δsbp1 strains under unstressed and sodium azide stress. Transcriptome analysis identified altered abundance of many transcripts belonging to stress-responsive pathways which were further validated by qRT-PCR results. Abundance of several transcripts was altered in Δscd6/Δsbp1 under normal conditions and upon stress. Overall, this study provides critical insights into transcriptome changes in response to sodium azide stress and the role of RGG-motif proteins in these changes.

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Sodium azide-induced mutagenesis in Saccharomyces cerevisiae

Cited by 17 publications

References 12 publications

The Pseudokinase Domain of Saccharomyces cerevisiae Tra1 Is Required for Nuclear Localization and Incorporation into the SAGA and NuA4 Complexes

The Pseudokinase Domain of Saccharomyces cerevisiae Tra1 Is Required for Nuclear Localization and Incorporation into the SAGA and NuA4 Complexes

Plant Dependent Mutation Assays

Elucidation of the RNA-granule inducing sodium azide stress response through transcriptome analysis

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