Thirty commercially available yeast cell wall products and two reference bentonites were tested for their ability to bind aflatoxin B(1) (AFB1) and zearalenone (ZON) in buffer solutions at pH 3 and pH 6.5 as well as in real gastric juice. For most products, the binding efficacy of AFB1 correlated with the ash content, which was between 2.6 and 89%, and constituted the inorganic non-volatile components, such as mineral clays, of the samples. Samples with smectite as the main ash component showed the highest binding efficacy; yet, a correlation with the content of mannanooligosaccharides (MOS) and β-glucans from yeast cell walls was not observed. Products containing >30% ash showed AFB1 adsorption values >90% at least in one of the investigated media whereas most products with <10% ash did not exceed adsorption rates of 20%. In the case of ZON, adsorption efficiency ranged between 10 and 60%. It tended to be lowest for products with MOS and β-glucan contents <10% and greatest for products with MOS and β-glucan contents >50%. However, there was no general correlation between the adsorption of ZON and the concentration of MOS and β-glucans. Different products of one brand sold in different countries were observed to bind AFB1 to different degrees, which was explained by the difference in ash contents and mineral composition. In the case of ZON, differences in adsorption between products of the same brand were less pronounced.
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http://dx.doi.org/10.1080/19440049.2011.630679 | DOI Listing |
Proc Natl Acad Sci U S A
February 2025
Laboratory of Molecular Biology, National Cancer Institute, NIH, Bethesda, MD 20892.
Hsp70, Hsp90, and ClpB/Hsp100 are molecular chaperones that help regulate proteostasis. Bacterial and yeast Hsp70s and their cochaperones function synergistically with Hsp90s to reactivate inactive and aggregated proteins by a mechanism that requires a direct interaction between Hsp90 and Hsp70 both in vitro and in vivo. and yeast Hsp70s also collaborate in bichaperone systems with ClpB and Hsp104, respectively, to disaggregate and reactivate aggregated proteins and amyloids such as prions.
View Article and Find Full Text PDFPLoS One
January 2025
Department of Bioinformatics, Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran.
Exophiala spinifera strain FM, a black yeast and melanized ascomycete, shows potential for oil biodesulfurization by utilizing dibenzothiophene (DBT) as its sole sulfur source. However, the specific pathway and enzymes involved in this process remain unclear due to limited genome sequencing and metabolic understanding of E. spinifera.
View Article and Find Full Text PDFMol Biol Cell
January 2025
Department of Biology, Institute of Biochemistry, ETH (Eidgenössische Technische Hochschule) Zürich, 8093 Zürich, Switzerland.
Biomolecular condensation has emerged as an important mechanism to control various cellular processes through the formation of membraneless organelles. Fluorescent protein tags have been extensively used to study the formation and the properties of condensates and , but there is evidence that tags may perturb the condensation properties of proteins. In this study, we carefully assess the effects of protein tags on the yeast DEAD-box ATPase Dhh1, a central regulator of processing bodies (P-bodies), which are biomolecular condensates involved in mRNA metabolism.
View Article and Find Full Text PDFmBio
January 2025
Department of Microbiology and Immunology, University of Rochester Medical Center, Rochester, New York, USA.
Unlabelled: Pathogenic strains cause cholera using different mechanisms. O1 and O139 serogroup strains use the toxin-co-regulated pilus (TCP) and cholera toxin (CT) for intestinal colonization and to promote secretory diarrhea, while non-O1/non-O139 serogroup strains are typically non-toxigenic and use alternate virulence factors to cause a clinically similar disease. An O39 serogroup, TCP/CT-negative strain, named AM-19226, uses a type III secretion system (T3SS) to translocate more than 10 effector proteins into the host cell cytosol.
View Article and Find Full Text PDFNucleic Acids Res
January 2025
College of Life Sciences, Beijing Normal University, Beijing 100875, China.
Mammalian J-domain protein DNAJC9 interacts with histones H3-H4 and is important for cell proliferation. However, its exact function remains unclear. Here, we show that, in the fission yeast Schizosaccharomyces pombe, loss of Djc9, the ortholog of DNAJC9, renders the histone chaperone Asf1 no longer essential for growth.
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