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Identification and Characterization of Two Aryl Sulfotransferases from Deep-Sea Marine Fungi and Their Implications in the Sulfation of Secondary Metabolites.
Mar Drugs
December 2024
Univ Brest, INRAE, Laboratoire Universitaire de Biodiversité et Écologie Microbienne, F-29280 Plouzané, France.
Sulfation plays a critical role in the biosynthesis of small molecules, regulatory mechanisms such as hormone signaling, and detoxification processes (phase II enzymes). The sulfation reaction is catalyzed by a broad family of enzymes known as sulfotransferases (SULTs), which have been extensively studied in animals due to their medical importance, but also in plant key processes. Despite the identification of some sulfated metabolites in fungi, the mechanisms underlying fungal sulfation remain largely unknown.
View Article and Find Full Text PDFPhotoactivatable O-GlcNAc Transferase Library Enables Covalent Chemical Capture of Solvent-Exposed TPR Domain Interactions.
Chembiochem
January 2025
Department of Chemistry, St. Olaf College, 1520 St. Olaf Ave., Northfield, MN, 55057.
O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT) is an essential, stress-sensing enzyme responsible for adding the O-GlcNAc monosaccharide to thousands of nuclear and cytoplasmic proteins to regulate cellular homeostasis. OGT substrates are found in almost all intracellular processes, and perturbations in protein O-GlcNAc levels have been implicated in proteostatic diseases, such as cancers, metabolic disorders, and neurodegeneration. This broad disease activity makes OGT an attractive therapeutic target; however, the substrate diversity makes pan-inhibition as a therapeutic strategy unfeasible.
View Article and Find Full Text PDFAnalytical tools to assess polymer biodegradation: A critical review and recommendations.
Sci Total Environ
December 2024
Battelle Memorial Institute, 505 King Ave, Columbus, OH 43201, United States. Electronic address:
Many petroleum-derived plastic materials are highly recalcitrant and persistent in the environment, posing significant threats to human and ecological receptors due to their accumulation in ecosystems. In recent years, research efforts have focused on advancing biological methods for polymer degradation. Enzymatic depolymerization has emerged as particularly relevant for biobased plastic recycling, potentially scalable for industrial use.
View Article and Find Full Text PDFSelective colonization of microplastics, wood and glass by antimicrobial-resistant and pathogenic bacteria.
Microbiology (Reading)
October 2024
European Centre for Environment and Human Health, Environment and Sustainability Institute, University of Exeter Medical School, Faculty of Health and Life Sciences, Penryn Campus, Cornwall, UK.
Article Synopsis
- The Plastisphere refers to the unique microbial communities that form on plastic debris, distinct from those on natural materials, which may harbor both pathogenic and antimicrobial-resistant (AMR) bacteria.
- Previous research lacked proper comparisons to natural substrates, leading to insufficient evidence about the unique threats posed by microplastics in spreading AMR pathogens.
- This study found that polystyrene and wood particles significantly enriched AMR bacteria, highlighting the role of particle roughness in colonization, but surface weathering of polyethylene did not notably affect AMR levels.
Principles of paralog-specific targeted protein degradation engaging the C-degron E3 KLHDC2.
Nat Commun
October 2024
Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN, 38105, USA.
PROTAC® (proteolysis-targeting chimera) molecules induce proximity between an E3 ligase and protein-of-interest (POI) to target the POI for ubiquitin-mediated degradation. Cooperative E3-PROTAC-POI complexes have potential to achieve neo-substrate selectivity beyond that established by POI binding to the ligand alone. Here, we extend the collection of ubiquitin ligases employable for cooperative ternary complex formation to include the C-degron E3 KLHDC2.
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