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pH-induced conformational changes in the selectivity filter of a potassium channel lead to alterations in its selectivity and permeation properties.
Front Pharmacol
January 2025
IDiBE-Instituto de Investigación, Desarrollo e Innovación en Biotecnología Sanitaria de Elche, Universidad Miguel Hernández, Elche, Spain.
The Selectivity Filter (SF) in tetrameric K channels, has a highly conserved sequence, TVGYG, at the extracellular entry to the channel pore region. There, the backbone carbonyl oxygens from the SF residues, create a stack of K binding sites where dehydrated K binds to induce a conductive conformation of the SF. This increases intersubunit interactions and confers a higher stability to the channel against thermal denaturation.
View Article and Find Full Text PDFDeltacoronavirus HKU11, HKU13, PDCoV (HKU15) and HKU17 spike pseudoviruses enter avian DF-1 cells via clathrin-mediated endocytosis in a Rab5-, Rab7- and pH-dependent manner.
Vet Res
January 2025
Guangdong Laboratory for Lingnan Modern Agriculture, College of Veterinary Medicine, South China Agricultural University, Guangzhou, China.
Porcine deltacoronavirus (PDCoV), also known as HKU15, is a swine enteropathogenic virus that is believed to have originated in birds. PDCoV belongs to the genus Deltacoronavirus (DCoV), the members of which have mostly been identified in diverse avian species. We recently reported that chicken or porcine aminopeptidase N (APN), the major cellular receptor for PDCoV, can mediate cellular entry via three pseudotyped retroviruses displaying spike proteins from three avian DCoVs (HKU11, HKU13, and HKU17).
View Article and Find Full Text PDFThe structural organisation of pentraxin-3 and its interactions with heavy chains of inter-α-inhibitor regulate crosslinking of the hyaluronan matrix.
Matrix Biol
January 2025
Manchester Cell-Matrix Centre, Division of Cell-Matrix Biology and Regenerative Medicine, School of Biological Sciences, Faculty of Biology, Medicine and Health, University of Manchester, Manchester Academic Health Science Centre, Manchester M13 9PT, UK; Lydia Becker Institute of Immunology and Inflammation, University of Manchester, Manchester, M13 9PL, United Kingdom. Electronic address:
Pentraxin-3 (PTX3) is an octameric protein, comprised of eight identical protomers, that has diverse functions in reproductive biology, innate immunity and cancer. PTX3 interacts with the large polysaccharide hyaluronan (HA) to which heavy chains (HCs) of the inter-α-inhibitor (IαI) family of proteoglycans are covalently attached, playing a key role in the (non-covalent) crosslinking of HC•HA complexes. These interactions stabilise the cumulus matrix, essential for ovulation and fertilisation in mammals, and are also implicated in the formation of pathogenic matrices in the context of viral lung infections.
View Article and Find Full Text PDFRegulatory dynamics of Sch9 in response to cytosolic acidification: From spatial reconfiguration to cellular adaptation to stresses.
iScience
January 2025
Department of Biology, Graduate School of Science, Chiba University, Chiba 263-8522, Japan.
The regulation of cellular metabolism is crucial for cell survival, with Sch9 in serving a key role as a substrate of TORC1. Sch9 localizes to the vacuolar membrane through binding to PI(3,5)P, which is necessary for TORC1-dependent phosphorylation. This study demonstrates that cytosolic pH regulates Sch9 localization.
View Article and Find Full Text PDFReplacement of the essential catalytic aspartate with serine leads to an active form of copper-containing nitrite reductase from the denitrifier Sinorhizobium meliloti 2011.
Biochim Biophys Acta Proteins Proteom
December 2024
Departamento de Física, Facultad de Bioquímica y Ciencias Biológicas, Universidad Nacional del Litoral and CONICET, S3000ZAA Santa Fe, Argentina.
Article Synopsis
- The study details the characterization of a mutated variant of copper-containing nitrite reductase (SmNirK) from S. meliloti, where the catalytic aspartate (Asp) is replaced with serine (Ser) via site-directed mutagenesis.
- The D134S variant retains the homotrimer structure and similar T1 electron transfer center to the wild-type, but shows altered electronic properties in the T2 active site, impacting its enzymatic efficiency and pH dependence.
- EPR studies reveal significant changes in the T2 properties due to the mutation, highlighting the role of T2 ligands in catalysis and suggesting a potential mechanism for electron transfer influenced by the Asp/Ser switch.
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