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The SGD provides internet access to the complete Saccharomyces cerevisiae genomic DNA sequence, its genes and their products, the phenotypes of its mutants, and the literature supporting these data. In the peer-reviewed literature report, experimental results on function and interaction of yeast genes are extracted by high-quality manual ...
Saccharomyces cerevisiae was the first eukaryotic organism to have its complete genome sequence determined.. This list of "sequenced" eukaryotic genomes contains all the eukaryotes known to have publicly available complete nuclear and organelle genome sequences that have been sequenced, assembled, annotated and published; draft genomes are not included, nor are organelle-only sequences.
Saccharomyces cerevisiae (/ ˌ s ɛr ə ˈ v ɪ s i. iː /) (brewer's yeast or baker's yeast) is a species of yeast (single-celled fungal microorganisms). The species has been instrumental in winemaking, baking, and brewing since ancient times.
This list of sequenced fungi genomes contains all the fungal species known to have publicly available complete genome sequences that have been assembled, annotated and published; draft genomes are not included, nor are organelle only sequences.
The Gal4 transcription factor is a positive regulator of gene expression of galactose-induced genes. [1] This protein represents a large fungal family of transcription factors, Gal4 family, which includes over 50 members in the yeast Saccharomyces cerevisiae e.g. Oaf1, Pip2, Pdr1, Pdr3, Leu3.
In Saccharomyces cerevisiae the U2 snRNA is associated with 18 polypeptides, seven of which are structural proteins common to all Sm class snRNPs. [11] These non-specific structural proteins associate with Sm snRNAs through a highly conserved recognition sequence (AU n G,n = 4-6) located within the RNA called Sm-binding sites. [12]
Pages in category "Saccharomyces cerevisiae genes" The following 39 pages are in this category, out of 39 total. This list may not reflect recent changes. A.
A Saccharomyces cerevisiae RAD52 mutant allele expressing a C-terminal truncated protein was found to complement other RAD52 mutant missense alleles. [26] This finding of intragenic complementation suggests that the RAD52 protein has a multimeric structure that allows cooperative interactions between the constituent monomers.