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S. cerevisiae does not excrete proteases, so extracellular protein cannot be metabolized. Yeasts also have a requirement for phosphorus , which is assimilated as a dihydrogen phosphate ion, and sulfur , which can be assimilated as a sulfate ion or as organic sulfur compounds such as the amino acids methionine and cysteine.
Autophagy-related protein 8 (Atg8) is a ubiquitin-like protein required for the formation of autophagosomal membranes. The transient conjugation of Atg8 to the autophagosomal membrane through a ubiquitin -like conjugation system is essential for autophagy in eukaryotes .
This transmission of protein state represents an epigenetic phenomenon where information is encoded in the protein structure itself, instead of in nucleic acids. Several prion-forming proteins have been identified in fungi, primarily in the yeast Saccharomyces cerevisiae. These fungal prions are generally considered benign, and in some cases ...
The protein complex [nb 1] SCF β-TrCP1/2 is an E3 ubiquitin ligase that functions in Wee1A ubiquitination. The M-phase kinases Polo-like kinase (Plk1) and Cdc2 phosphorylate two serine residues in Wee1A which are recognized by SCF β-TrCP1/2. [22] S. cerevisiae homologue Swe1
In Saccharomyces cerevisiae (Baker's yeast), CAP is a component of the adenylyl cyclase complex (Cyr1p) that serves as an effector of Ras during normal cell signalling. S. cerevisiae CAP functions to expose adenylate cyclase binding sites to Ras, thereby enabling adenylate cyclase to be activated by Ras regulatory signals.
A 3D representation of the RRM3 protein, as modelled by SWISS-MODEL. RRM3 is a gene that encodes a 5′-to-3′ DNA helicase [1] known affect multiple cellular replication and repair processes and is most commonly studied in Saccharomyces cerevisiae. RRM3 formally stands for Ribosomal DNArecombination mutation 3. [1]
In the yeast Saccharomyces cerevisiae, the MSH2, MLH1 and PMS1 proteins are required for repair of DNA base pair mismatches, thus contributing to mutation avoidance. [7] The MLH1 and PMS1 proteins physically associate, likely forming a heterodimer which then interacts with the MSH2 protein to form a ternary complex that acts in the initiation of DNA mismatch repair. [7]
Sic1, a protein, is a stoichiometric inhibitor [1] of Cdk1-Clb (B-type cyclins) complexes in the budding yeast Saccharomyces cerevisiae.Because B-type cyclin-Cdk1 complexes are the drivers of S-phase initiation, Sic1 prevents premature S-phase entry. [2]