Search

Although proline is the most or second most abundant amino acid in wort and grape must, it is not fully consumed by the yeast Saccharomyces cerevisiae during alcoholic fermentation, unlike other amino acids. Our previous studies showed that arginine, the third most abundant amino acid in wort, inhibits the utilization of proline in most strains of S. cerevisiae. Furthermore, we found that some non-Saccharomyces yeasts utilized proline in a specific artificial medium with arginine and proline as the only nitrogen source, but these yeasts were not suitable for beer fermentation due to their low alcohol productivity. For yeasts to be useful for brewing, they need to utilize proline and produce alcohol during fermentation. In this study, 11 S. cerevisiae strains and 10 non-Saccharomyces yeast strains in the Phaff Yeast Culture Collection were identified that utilize proline effectively. Notably, two of these S. cerevisiae strains, UCDFST 40-144 and 68-44, utilize proline and produce sufficient alcohol in the beer fermentation model used. These strains have the potential to create distinctive beer products that are specifically alcoholic but with a reduction in proline in the finished beer.

The baking industry is experiencing significant growth, primarily due to the widespread adoption of frozen dough baking. However, this process can negatively impact the fermentation ability of yeast, as freezing can induce stress in yeast cells. This study reports the molecular interplay between the ubiquitin–proteasome system and freezing stress tolerance in the yeast Saccharomyces cerevisiae. Using the proteasome inhibitor MG132, we first screened mutants with enhanced freezing stress tolerance. Three mutants showed elevated activity of the intracellular proteasome, particularly trypsin-like activity (more than threefold) and reduced sensitivity to MG132 inhibition of chymotrypsin-like activity (less than 0.125-fold). Genomic analysis of these mutants revealed mutations in the ROX1 gene, a heme-dependent repressor of hypoxic genes. Importantly, the ROX1 deletion strain displayed slightly improved freezing stress tolerance (about 1.5-fold). Comprehensive transcription analysis identified the ANB1 gene as a potential downstream target of Rox1. Overexpression of ANB1 enhanced freezing stress tolerance (about 1.5-fold) with increased the proteasome's activity, indicating that Rox1 contributes to changes in the proteasome's activity and freezing stress tolerance through the function of Anb1. The present data provide new insights into the mechanisms of freezing stress tolerance and help us improve the baking of frozen dough to produce higher-quality bread. [ABSTRACT FROM AUTHOR]

Aims: This study aimed to establish a yeast‐based screening system for potential compounds that can alleviate the toxicity of α‐synuclein (α‐syn), a neuropathological hallmark of Parkinson's disease, either inhibition of α‐syn aggregation or promotion of ubiquitin‐mediated degradation of α‐syn. Methods and Results: A powerful yeast‐based screening assay using the rsp5A401E‐mutant strain, which is hypersensitive to α‐syn aggregation, was established by two‐step gene replacement and further overexpressed the GFP‐fused α‐syn in the drug‐sensitive yeast strain with a galactose‐inducible multicopy plasmid. The rsp5A401E‐mutant strain treated with baicalein, a known α‐syn aggregation inhibitor, showed better α‐syn toxicity alleviation than the same background wild type strain as accessed by comparison on the reduction kinetics of viable dye resazurin fluorometrically (λex540/λem590 nm). The rsp5A401E‐mutant yeast‐based assay system showed high sensitivity as it could detect as low as 3.13 µmol l−1 baicalein, the concentration that lower than previously report detected by the in vitro assay. Conclusions: Our yeast‐based system has been effective for screening potential compounds that can alleviate α‐syn toxicity with high sensitivity and specificity. Significance and Impact of the Study: Yeast‐based assay system can be used to discover novel neuroprotective drug candidates which may be either efficiently suppress‐α‐syn aggregation or enhance ubiquitin‐dependent degradation. [ABSTRACT FROM AUTHOR]

Arginine is a proteinogenic amino acid that organisms additionally exploit both for nitrogen storage and as a stress protectant. The location of arginine, whether intra- or extracellular, is important in maintaining physiological homeostasis. Here, we identified an arginine transporter ortholog of the emerging fungal pathogenic Candida glabrata. Blast searches revealed that the C. glabrata genome contains two potential orthologs of the Saccharomyces cerevisiae arginine transporter gene CAN1 (CAGL0J08162g and CAGL0J08184g). We then found that CAGL0J08162g is stably located on the plasma membrane and performs cellular uptake of arginine. Moreover, CAGL0J08162-disrupted cells of C. glabrata showed a partial resistance to canavanine, a toxic analog of arginine. Our data suggest that CAGL0J08162g is a key arginine transporter in the pathogenic C. glabrata (CgCan1).