Kluyveromyces marxianus is a thermotolerant yeast that has been explored for potential use in biotechnological applications, such as production of biofuels, single-cell proteins, enzymes, and other heterologous proteins. Here, we present the high-quality draft of the 10.9-Mb genome of K. marxianus var. marxianus KCTC 17555 (= CBS 6556 = ATCC 26548).
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http://dx.doi.org/10.1128/EC.00260-12 | DOI Listing |
FEBS J
December 2024
Department of Chemical Engineering, Texas A&M University, College Station, TX, USA.
The purine metabolism is crucial for cellular function and is a conserved metabolic network from prokaryotes to humans. While extensively studied in microorganisms like yeast and bacteria, the impact of perturbing dietary intermediates from the purine biosynthesis on animal development and growth remains poorly understood. We utilized Caenorhabditis elegans as the metazoan model to investigate the mechanisms underlying this deficiency.
View Article and Find Full Text PDFPlant Physiol Biochem
November 2024
State Key Laboratory for Crop Stress Resistance and High-Efficiency Production, College of Agronomy, Northwest A&F University, YangLing, 712100, Shaanxi, China. Electronic address:
PNAS Nexus
December 2024
Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.
GCN2 is a conserved receptor kinase activating the integrated stress response (ISR) in eukaryotic cells. The ISR kinases detect accumulation of stress molecules and reprogram translation from basal tasks to preferred production of cytoprotective proteins. GCN2 stands out evolutionarily among all protein kinases due to the presence of a histidyl-tRNA synthetase-like (HRSL) domain, which arises only in GCN2 and is located next to the kinase domain (KD).
View Article and Find Full Text PDFInt J Mol Sci
November 2024
Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, School of Life Sciences, Yunnan Normal University, Kunming 650500, China.
Catalase (CAT) plays a crucial role in plant responses to environmental stresses and maintaining redox homeostasis. However, its putative heat lability might compromise its activity and function, thus restricting plant thermotolerance. Herein, we verified Arabidopsis CAT3 was of poor thermostability that was then engineered by fusion expression in .
View Article and Find Full Text PDFPLoS Pathog
November 2024
Department of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, North Carolina, United States of America.
The eukaryotic serine/threonine protein phosphatase PP2A is a heterotrimeric enzyme composed of a scaffold A subunit, a regulatory B subunit, and a catalytic C subunit. Of the four known B subunits, the B"' subunit (known as striatin) interacts with the multi-protein striatin-interacting phosphatase and kinase (STRIPAK) complex. Orthologs of STRIPAK components were identified in Cryptococcus neoformans, namely PP2AA/Tpd3, PP2AC/Pph22, PP2AB/Far8, STRIP/Far11, SLMAP/Far9, and Mob3.
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