ArticleProceedings of the National Academy of Sciences of the United States of America2008
Genome-wide screen of Saccharomyces cerevisiae null allele strains identifies genes involved in selenomethionine resistance.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- A cysteinyl-tRNA synthetase variant confers resistance against selenite toxicity and decreases selenocysteine misincorporation.The Journal of biological chemistry · 2019Article
- A practical method for efficient and optimal production of Seleno-methionine-labeled recombinant protein complexes in the insect cells.Protein science : a publication of the Protein Society · 2019Article
- Exposure to selenomethionine causes selenocysteine misincorporation and protein aggregation in Saccharomyces cerevisiae.Scientific reports · 2017Article
- Biological Chemistry of Hydrogen Selenide.Antioxidants (Basel, Switzerland) · 2016Review
- Trans-sulfuration Pathway Seleno-amino Acids Are Mediators of Selenomethionine Toxicity in Saccharomyces cerevisiae.The Journal of biological chemistry · 2015Article
- Yeast as a model system to study metabolic impact of selenium compounds.Microbial cell (Graz, Austria) · 2015Review
- Cytotoxic mechanism of selenomethionine in yeast.The Journal of biological chemistry · 2012Article
- Article
- A novel 3-methylhistidine modification of yeast ribosomal protein Rpl3 is dependent upon the YIL110W methyltransferase.The Journal of biological chemistry · 2010Article
- Mutation of high-affinity methionine permease contributes to selenomethionyl protein production in Saccharomyces cerevisiae.Applied and environmental microbiology · 2010Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Selenomethionine (SeMet) is a potentially toxic amino acid, and yet it is a valuable tool in the preparation of labeled proteins for multiwavelength anomalous dispersion or single-wavelength anomalous dispersion phasing in X-ray crystallography. The mechanism by which high levels of SeMet exhibits its toxic effects in eukaryotic cells is not fully understood. Attempts to use Saccharomyces cerevisiae for the preparation of fully substituted SeMet proteins for X-ray crystallography have been limited. A screen of the viable S. cerevisiae haploid null allele strain collection for resistance to SeMet was performed. Deletion of the CYS3 gene encoding cystathionine gamma-lyase resulted in the highest resistance to SeMet. In addition, deletion of SSN2 resulted in both increased resistance to SeMet as well as reduced levels of Cys3p. A methionine auxotrophic strain lacking CYS3 was able to grow in media with SeMet as the only source of Met, achieving essentially 100% occupancy in total proteins. The CYS3 deletion strain provides advantages for an easy and cost-effective method to prepare SeMet-substituted protein in yeast and perhaps other eukaryotic systems.
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Registered trials
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