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Yeast

About: Yeast is a research topic. Over the lifetime, 31777 publications have been published within this topic receiving 868967 citations. The topic is also known as: yeasts.


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Journal ArticleDOI
TL;DR: Experiments in fission yeast and budding yeast have revealed the existence of highly intricate signaling networks that are required for regulation of Swe1, the budding yeast homolog of Wee1, and may provide important clues to how cell growth and cell division are coordinated.
Abstract: Wee1-related kinases function in a highly conserved mechanism that controls the timing of entry into mitosis. Loss of Wee1 function causes fission yeast and budding yeast cells to enter mitosis before sufficient growth has occurred, leading to formation of daughter cells that are smaller than normal. Early work in fission yeast suggested that Wee1 is part of a cell-size checkpoint that prevents entry into mitosis before cells have reached a critical size. Recent experiments in fission yeast and budding yeast have provided new support for this idea. In addition, studies in budding yeast have revealed the existence of highly intricate signaling networks that are required for regulation of Swe1, the budding yeast homolog of Wee1. Further understanding of these signaling networks may provide important clues to how cell growth and cell division are coordinated.

175 citations

Journal ArticleDOI
TL;DR: Yeast gene that encodes TSA showed no significant homology to any known catalase, SOD, or peroxidase enzymes, consistent with the observation that protector protein did not possess catalytic activity characteristic of these conventional antioxidant enzymes.
Abstract: We have previously purified a 25-kDa enzyme from yeast that prevents damage induced by the metalcatalyzed oxidation (MCO) system containing a thiol like dithiothreitol and 2-mercaptoehtanol (Fe3+, O2, and RSH) but not that induced by the MCO system containing ascorbate (Fe3+, O2, and ascorbate) [1]. Although the exact nature of the oxidant eliminated by the 25-kDa enzyme was not known at that time, its importance as an antioxidant was apparent as the application of oxidative pressure to yeast resulted in an increase in its synthesis, and the 25-kDa protein constituted 0.7% of total soluble protein from yeast grown aerobically [2]. Not knowing anything about the nature of chemical reaction catalyzed by the 25-kDa protein, we briefly called it “protector protein” and then “thiol-specific antioxidant (TSA)” because the enzyme provides protection against a thiol-containing oxidation system, but not against an oxidation system without thiol [1,2]. Yeast gene that encodes TSA was cloned and sequenced [3]. It showed no significant homology to any known catalase, SOD, or peroxidase enzymes. This lack of homology was consistent with the observation that protector protein did not possess catalytic activity characteristic of these conventional antioxidant enzymes. A yeast mutant that cannot produce TSA was constructed by homologous recombination [3]. The mutant and wild-type strains grew at equal rates under anaerobic conditions. However, under aerobic conditions, especially under oxidative stress, the growth rate of mutant yeast was significantly lower than that of wild-type yeast. TSA was not associated with any obvious redox cofactors. Rather, TSA contained two cysteine residues, which correspond to Cys47 and Cys170 in the yeast enzyme [4]. The two cysteines did not form an intramolecular disulfide. Instead, TSA existed predominantly as a dimer linked by two identical disulfide bonds between Cys47 and Cys170 as evidenced by direct isolation of dimeric tryptic peptides in which one monomer contains Cys47 and the other contains Cys170 [4]. A mutant with Cys47 replaced by Ser (C47S mutant) failed to protect glutamine synthetase from the thiol oxidation system, whereas wild type and C170S mutant were equally protective. Thus Cys47, but not Cys170, appeared to be the site of oxidation.

175 citations

Journal ArticleDOI
TL;DR: The antimicrobial properties of naturally occurring components of raw materials can be exploited to enhance the microbial stability of beer.
Abstract: While beer provides a very stable microbiological environment, a few niche microorganisms are capable of growth in malt, wort and beer. Growth of mycotoxin-producing fungi during malting, production of off-flavours and development of turbidity in the packaged product due to the growth and metabolic activity of wild yeasts, certain lactic acid bacteria (LAB) and anaerobic Gram negative bacteria, impact negatively on beer quality. It follows that any means by which microbial contamination can be reduced or controlled would be of great economic interest to the brewing industry and would serve the public interest. There has been an increasing effort to develop novel approaches to minimal processing, such as the exploitation of inhibitory components natural to raw materials, to enhance the microbiological stability of beer. LAB species, which occur as part of the natural barley microbiota, persist during malting and mashing, and can play a positive role in the beer-manufacturing process by their contribution to wort bioacidification or the elimination of undesirable microorganisms. Other naturally occurring components of beer that have been valued for their preservative properties are hop compounds. It may be possible to enhance the antimicrobial activities of these compounds during brewing. Some yeast strains produce and excrete extracellular toxins called zymocins, which are lethal to sensitive yeast strains. Yeast strains resistant to zymocins have been constructed. Imparting zymocinogenic activity to brewing yeast would offer a defence against wild yeasts in the brewery. Thus, the antimicrobial properties of naturally occurring components of raw materials can be exploited to enhance the microbial stability of beer.

175 citations

Journal ArticleDOI
TL;DR: Wright, B. E. & Shockman, G. D. (1955).
Abstract: Shockman, G. D. & Toennies, G. (1954). Arch. Biochem. Biophys. 50, 9. Stadtman, E. R., Novelli, G. D. & Lipmann, F. (1951). J. biol. Chem. 191, 365. Stekol, J. A. (1955). In Amino Acid Metabolism, p. 509. Ed. by McElroy, W. D. & Glass, H. B. Baltimore: Johns Hopkins Press. Stickland, L. H. (1951). J. gen. Microbiol. 5, 698. Szulmajster, J. & Woods, D. D. (1955). Abstr. 3rd int. Congr. Biochem., Brussels, p. 44. Toennies, G. & Shockman, G. D. (1953). Arch. Biochem. Biophys. 45, 447. Ve6efra, M. & Gaspari6, J. (1954). Coll. Trav. chim. Tche'cosl. 19, 1175. Viebock, F. & Brecher, C. (1930). Ber. dtsch. chem. Ges. 63, 3207. Wright, B. E. (1955a). Biochim. biophy8. Acta, 16, 165. Wright, B. E. (1955b). J. Amer. chem. Soc. 77, 3930. Wright, B. E. (1956). J. biol. Chem. 219, 873. Wright, B. E. (1958). Proc. 4th int. Congr. Biochem., Vienna, 11, 266. Wright, B. E. & Stadtman, T. C. (1956). J. biol. Chem. 219, 863.

175 citations

Journal ArticleDOI
TL;DR: The results revealed that top-fermenting beer yeasts are polyphyletic, with a main clade composed of at least three subgroups, dominantly represented by the German, British, and wheat beer strains.

175 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
20231,445
20223,214
2021816
2020870
2019977
2018968