Regulation of amino acid, nucleotide and phosphate metabolism in Saccharomyces cerevisiae
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TLDR
This review focuses on recent developments in the field of amino acid, nucleotide, and phosphate metabolism and provides illustrative examples of how yeast cells combine a variety of mechanisms to achieve coordinated regulation of multiple metabolic pathways.Abstract:
Ever since the beginning of biochemical analysis, yeast has been a pioneering model for studying the regulation of eukaryotic metabolism. During the last three decades, the combination of powerful yeast genetics and genome-wide approaches has led to a more integrated view of metabolic regulation. Multiple layers of regulation, from suprapathway control to individual gene responses, have been discovered. Constitutive and dedicated systems that are critical in sensing of the intra- and extracellular environment have been identified, and there is a growing awareness of their involvement in the highly regulated intracellular compartmentalization of proteins and metabolites. This review focuses on recent developments in the field of amino acid, nucleotide, and phosphate metabolism and provides illustrative examples of how yeast cells combine a variety of mechanisms to achieve coordinated regulation of multiple metabolic pathways. Importantly, common schemes have emerged, which reveal mechanisms conserved among various pathways, such as those involved in metabolite sensing and transcriptional regulation by noncoding RNAs or by metabolic intermediates. Thanks to the remarkable sophistication offered by the yeast experimental system, a picture of the intimate connections between the metabolomic and the transcriptome is becoming clear.read more
Citations
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Nutritional Control of Growth and Development in Yeast
TL;DR: The current understanding of the structures of the networks responsible for assessing the quantity and quality of carbon and nitrogen sources are reviewed and the profound knowledge on the structure of these signaling networks are highlighted.
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Nutrient sensing and signaling in the yeast Saccharomyces cerevisiae
Michaela Conrad,Joep Schothorst,Harish Nag Kankipati,Griet Van Zeebroeck,Marta Rubio-Texeira,Johan M. Thevelein +5 more
TL;DR: The yeast Saccharomyces cerevisiae has been a favorite organism for pioneering studies on nutrient-sensing and signaling mechanisms, and its discovery of nutrient transceptors (transporter receptors) as nutrient sensors has led to important new concepts and insight into nutrient-controlled cellular regulation.
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Nutrient sensing and TOR signaling in yeast and mammals
Asier González,Michael N. Hall +1 more
TL;DR: How nutrient availability is sensed and transduced to TOR in budding yeast and mammals is reviewed to allow novel strategies in the treatment for mTOR‐related diseases.
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Yeast Creates a Niche for Symbiotic Lactic Acid Bacteria through Nitrogen Overflow
Olga Ponomarova,Natalia Gabrielli,Daniel C. Sévin,Michael Mülleder,Katharina Zirngibl,Katsiaryna Bulyha,Sergej Andrejev,Eleni Kafkia,Athanasios Typas,Uwe Sauer,Markus Ralser,Kiran Raosaheb Patil +11 more
TL;DR: It is shown how yeast enables growth of lactic acid bacteria through endogenous, multi-component, cross-feeding in a readily established community, and how nitrogen overflow by yeast benefits L. plantarum in grape juice, and contributes to emergence of mutualism with L. lactis in a medium with lactose.
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Asymmetry in inward- and outward-affinity constant of transport explain unidirectional lysine flux in Saccharomyces cerevisiae.
Frans Bianchi,Joury S van 't Klooster,Stephanie J Ruiz,Katja Luck,Tjeerd Pols,Ina L. Urbatsch,Bert Poolman +6 more
TL;DR: The previously described unidirectional nature of lysine transport in S. cerevisiae is explained by the extraordinary kinetics of Lyp1 and the high asymmetry in transport together with secondary storage in the vacuole allow the cell to accumulate basic amino acids to very high levels.
References
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An αβ T cell receptor structure at 2.5 Å and its orientation in the TCR-MHC complex
K. Christopher Garcia,Massimo Degano,Robyn L. Stanfield,Anders Brunmark,Michael R. Jackson,Per A. Peterson,Luc Teyton,Ian A. Wilson +7 more
TL;DR: In this article, the x-ray structure of the complete extracellular fragment of a glycosylated αβ T cell receptor (TCR) was determined at 2.5 angstroms, and its orientation bound to a class I MHC-peptide (pMHC) complex was elucidated from crystals of the TCR- pMHC complex.