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Integration of heterologous enzymes into the reaction chambers of fungal fatty acid synthases (FASs) demonstrates the capacity of these megaenzymes for engineered production of short- and medium-chain fatty acids and methyl ketones.
Pharmacological chaperones improve folding of destabilized Escherichia coli dihydrofolate reductase (DHFR) and human disease-linked α-galactosidase A (α-GAL) by biasing the kinetic partitioning between folding, aggregation, and degradation. Chaperoning spares DHFR from aggregation and α-GAL from degradation.
In vitro and in silico analysis enables the rational design of fatty acid synthase (FAS)-mediated pathways for the compartmentalized production of desirable fatty acids and a polyketide lactone.
Discovery and characterization of an unusually permissive C-prenyltransferase provides a biocatalytic route for generating novel prenylated compounds, including daptomycin derivatives with increased potency.
A structural study of MraY, an essential enzyme from Clostridium bolteae involved in bacterial cell wall synthesis, in complex with the natural product antibiotic tunicamycin, provides a basis for future antibiotic design.
The combination of an extremely soluble chimeric spider silk protein (spidroin) and a biomimetic spinning method that recapitulates the endogenous pH gradient in silk glands produces a remarkably strong artificial spider silk.
The synergistic effect of the GPCR β2AR on signaling through another GPCR, PTHR, is explained by the release of Gβγ from the heterotrimeric Gαiβγ protein, activating adenylate cyclase AC2 and subsequent prolonged cAMP signaling in internal compartments
The development of small-molecule fluorescent probes through addition of a lipidated cysteine residue next to a caged fluorophore enables detection of endogenous cysteine depalmitoylation by acyl–protein thioesterases in vitro and in live cells.
The iron protein components of bacterial nitrogenases are capable of reducing carbon dioxide (CO2) to carbon monoxide (CO) in the absence of their catalytic partners, mimicking the activity of CO dehydrogenase.
Small-molecule control of transcriptional activation and genome editing was achieved by tethering inducible protein degron domains to an engineered CRISPR–Cas9 system.
A genetic screening approach using chemically mutagenized haploid mouse embryonic stem cells combined with next-generation sequencing identified recessive suppressor point mutations that elicit resistance to 6-thioguanine.
Mass spectrometry analysis of stromal extracts reveal a peptidolytic cascade in the plant chloroplast consisting of oligopeptidases and aminopeptidases that mediates the complete degradation of signal peptides to free amino acids.
Unlike their bacterial counterparts, fungal nonribosomal peptide synthetases utilize a terminal condensation-like (CT) domain to form macrocycles, details of which are illuminated by structures of a CT domain and neighboring thiolation domain.
The synthetic bioinformatic natural products (syn-BNPs) approach identifies putative natural products that are validated directly by independent synthesis. Its application led to the identification of humimycins, non-ribosomal peptides that have antimicrobial activity in mice.
ADP-ribosylation is a post-translational protein modification that regulates numerous cellular pathways. An approach involving histone purification, partial filter-aided digestion and ETD mass spectrometry reveals that serine residues in histone proteins are ADP-ribosylated.
A proteomic approach in Saccharomyces cerevisiae identifies cytochrome b reductase (Cbr1) as an NADH-dependent electron donor for diphthamide biosynthesis 3 (Dph3), a protein that serves as an electron source for diphthamide biosynthesis and tRNA modification.
A chemoproteomics approach utilizing the thermal shift assay and quantitative MS resulted in the identification of phenylalanine hydroxylase as an off-target of the histone deacetylase inhibitor panobinostat.
Nikkomycins and polyoxins are peptidylnucleosides with antifungal activity. The biosynthetic routes to these natural products share a bicyclic intermediate formed by a carbon radical–centered ring closure catalyzed by the radical SAM enzymes NikJ or PolH.
A high-throughput screen against the E. coli tetracycline-resistance efflux pump TetA identifies two ‘selection-inverting’ compounds that swap tetracycline resistance for resistance to another antibiotic, paving the way for two-phase antibiotic treatment protocols.
