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The GlycoSCORES method, which involves cell-free protein expression and substrate-site profiling of glycosyltransferase enzymes by SAMDI–MS, enables the identification of glycosylation tags for glycoengineering efforts.
A β-lactamase, a novel type of amidase, and the phenylacetic acid catabolon comprise a catabolic pathway, revealed by genomic and transcriptomic analysis, that enables multiple soil bacteria to use β-lactam antibiotics as a carbon source.
The monomeric near-infrared (NIR) fluorescent protein miRFP720 enables development of fully NIR Förster resonance energy transfer (FRET) biosensors compatible with CFP–YFP FRET biosensors and blue–green optogenetic tools without optical cross-talk.
Ancestral sequence inference, directed evolution, structural analysis, NMR, and molecular dynamics simulations illuminate how enantioselective activity arises during the evolutionary trajectory of chalcone isomerase from a noncatalytic ancestor.
Ancestral protein reconstruction, with structural and biochemical analysis, illustrates the evolution of a solute-binding protein to cyclohexadienyl dehydratase through incorporation of a catalytic residue and gradual reshaping of the binding site.
Use of a combined Tn-seq and machine-learning approach for predicting mechanisms and targets of antibiotic action in Staphylococcus aureus shows that the natural product lysocin E (LysE) binds Lipid II on the cell surface and damages the membrane.
A phage-derived peptide selectively binds to the Frizzled 7 CRD resulting in disruption of the dimer interface and impairing Wnt/β-catenin stem signaling in intestinal organoids.
The jasmonoyl-isoleucine (JA-Ile) receptor COI1 is functionally conserved between the bryophyte Marchantia polymopha and the eudicot Arabidopsis thaliana, with two isomers of the JA-Ile precursor dinor-OPDA acting as the ligand for Marchantia COI1.
An ornithine–ammonia cycle involving an arginine dihydrolase was identified in cyanobacteria. This cycle serves as a conduit in the nitrogen storage-and-remobilization machinery and enables cellular adaptation to nitrogen fluctuations.
Crystal structures of a subunit of the ubiquitin ligase complex serving the N-end rule pathway of degrons marked by proline define a degron recognition mechanism and selection criteria for substrates.
Comprehensive glycome profiling of immunoglobulin G (IgG) in 95 strains of mice from the Collaborative Cross genetics resource reveals the extent and variability of IgG glycosylation in vivo.
Dissolved oxygen and a reducing-plus-oxidizing system suppress photobleaching and photoblinking in single-molecule tracking experiments, allowing long recordings of CD47 and integrin that showed temporary immobilization within focal adhesions.
The crystal structure and cryo-electron microscopy of the loading/condensing region of a nonreducing polyketide synthase reveals the insertion of a starter-unit acyltransferase into the condensing region and an asymmetrical post-loading state.
FINO2 is a small molecule that requires the endoperoxide moiety and hydroxyl group to promote ferroptosis through indirect inhibition of GPX4 enzymatic function and direct oxidation of iron, resulting in increased lipid peroxidation.
A single-molecule forced unfolding of E. coli chloride transporter ClC-ec1 shows that the N- and C-terminal halves of the protein unfold independently, with exposed polar surfaces stabilized by membrane lipid head groups and water.
The biosynthesis and secretion of redox-active coumarins sideretin and fraxetin in Arabidopsis thaliana enables the plant to acquire iron under nutrient-limited conditions and provides a blueprint for the use of related compounds in other eudicots.
The dTAG system pairs potent heterobifunctional degraders and extensible tagging strategies to achieve immediate and reversible degradation of divergent proteins, facilitating biological investigation and drug target validation in cells and in mice.
The crystal structure of a methyltransferase domain embedded within an interrupted adenylation domain provides insight into how a nonribosomal peptide synthetase N-methylates amino acid precursors for their incorporation into the peptide product.