The surface of polytetrafluoroethylene (PTFE) was modified using plasma immersion ion implantation (PIII) with the aim of improving its ability to immobilize yeast. The density of immobilized cells on PIII-treated and -untreated PTFE was compared as a function of incubation time over 24 h. Rehydrated yeast cells attached to the PIII-treated PTFE surface more rapidly, with higher density, and greater attachment strength than on the untreated surface. The immobilized yeast cells were removed mechanically or chemically with sodium hydroxide and the residues left on the surfaces were analysed with Fourier transform infrared spectroscopy-attenuated total reflection (FTIR-ATR) and X-ray photoelectron spectroscopy (XPS). The results revealed that the mechanism of cell attachment on both surfaces differs and a model is presented for each. Rapid attachment on the PIII-treated surface occurs through covalent bonds of cell wall proteins and the radicals on the treated surface. In contrast, on the untreated surface, only physisorbed molecules were found in the residue and lipids were more highly concentrated than proteins. The presence of lipids in the residue was found to be a consequence of damage to the plasma membrane during the rehydration process and the increased cell stress was also apparent by the amount of Hsp12 in the protein residue. The immobilized yeast cells on PIII-treated PTFE were found to be as active as yeast cells in suspension.
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http://dx.doi.org/10.1098/rsif.2012.0347 | DOI Listing |
Nat Commun
January 2025
Center for Biomolecular and Cellular Structure, Institute for Basic Science (IBS), Daejeon, Republic of Korea.
Toxic protein aggregates are associated with various neurodegenerative diseases, including Huntington's disease (HD). Since no current treatment delays the progression of HD, we develop a mechanistic approach to prevent mutant huntingtin (mHttex1) aggregation. Here, we engineer the ATP-independent cytosolic chaperone PEX19, which targets peroxisomal membrane proteins to peroxisomes, to remove mHttex1 aggregates.
View Article and Find Full Text PDFFEMS Yeast Res
January 2025
Department of Life Sciences, Chalmers University of Technology, 412 58 Gothenburg, Sweden.
Yeast-based sensors have shown great applicability for deorphanization of G protein-coupled receptors (GPCRs) and screening of ligands targeting these. A GPCR of great interest is free fatty acid 2 receptor (FFA2R), for which short-chain fatty acids such as propionate and acetate are agonists. FFA2R regulates a wide array of downstream receptor signaling pathways in both adipose tissue and immune cells and has been recognized as a promising therapeutic target, having been implicated in several metabolic and inflammatory diseases.
View Article and Find Full Text PDFPLoS One
January 2025
SLAC National Accelerator Laboratory, Stanford University, Stanford, California, United States of America.
Protein-Protein Interactions (PPIs) are a key interface between virus and host, and these interactions are important to both viral reprogramming of the host and to host restriction of viral infection. In particular, viral-host PPI networks can be used to further our understanding of the molecular mechanisms of tissue specificity, host range, and virulence. At higher scales, viral-host PPI screening could also be used to screen for small-molecule antivirals that interfere with essential viral-host interactions, or to explore how the PPI networks between interacting viral and host genomes co-evolve.
View Article and Find Full Text PDFGenes Cells
January 2025
Department of Genetic Biochemistry, The National Institutes of Biomedical Innovation, Health and Nutrition, Shinjuku-ku, Tokyo, Japan.
Catalytic subunit of DNA polymerase ζ (REV3), involved in translesion-replication is evolutionarily conserved from yeast and plants to higher eukaryotes. However, a large intermediate domain is inserted in REV3 of humans and mice. The domain has "DUF4683" region, which is significantly similar to human neurite extension and migration factor (NEXMIF).
View Article and Find Full Text PDFAngew Chem Int Ed Engl
January 2025
Boston College, Chemistry, 2609 Beacon Street, 201 Merkert Chemistry Center, 02467, Chestnut hill, UNITED STATES OF AMERICA.
Site-specific incorporation of noncanonical amino acids (ncAAs) into proteins in eukaryotes has predominantly relied on the pyrrolysyl-tRNA synthetase/tRNA pair. However, access to additional easily engineered pairs is crucial for expanding the structural diversity of the ncAA toolbox in eukaryotes. The Escherichia coli-derived leucyl-tRNA synthetase (EcLeuRS)/tRNA pair presents a particularly promising alternative.
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