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A sensor of membrane depolarization controls the activity of a bound enzyme through a novel mechanism involving two sequential voltage-dependent transitions allosterically coupled to changes in the substrate specificity of the catalytic domain.
Bacterial pathogen–secreted proteases may have a key role in inhibiting a potentially widespread host-pathogen interaction. Activity-based protein profiling enabled the identification of a major Vibrio cholerae serine protease that limits the ability of a host-derived intestinal lectin to bind to the bacterial pathogen in vivo.
Cdk1 links mitotic entry to faithful chromosome segregation by activating the acetyltransferase TIP60. Acetylation of Aurora B kinase by TIP60 protects Aurora B's activation loop from dephosphorylation by the PP2A phosphatase to ensure robust Aurora B activation.
Kinesin is a motor protein that drives intracellular transport by stepping along microtubules in a hand-over-hand manner. Advanced dark-field microscopy has made it possible to capture the gait of this motor with unprecedented resolution.
This Review article highlights bacterial toxin-antitoxin system components, their function and the mechanisms they use to affect diverse physiological functions and conditions, including dormancy and entry and exit from the persistent state defined by a high tolerance to antibiotics.
YihQ hydrolyzes the glycosidic linkage in sulfoquinovosyl diacylglyceride (SQDG) to form sulfoquinovose (SQ). Crystal structure analysis reveals active site residues required for the specificity of YihQ for SQ and allows the identification of other YihQ homologs.
Two chemical series, oxalamides and benozothiazoles, produced toxicity in particular lung cancer cells. These compounds were metabolized in these sensitive cells by the cytochrome P450 enzyme CYP4F11 into potent inhibitors of stearoyl CoA desaturase.
The cell cycle regulator CDK1 phosphorylates the acetyltransferase TIP60, which subsequently acetylates the mitotic regulator Aurora B to ensure chromosomal segregation. Aurora B acetylation prevents inactivation by PP2A-mediated dephosphorylation.
A retrobiosynthetic algorithm that relates known antibiotics by the similarities of their biosynthetic pathways to cluster them into distinct classes. Focusing on the telomycins helps to define the mechanism of action of this antibiotic class.
A structural and functional study including a mutational analysis of C. elegans POFUT2 with GDP and a peptide substrate helps explain how this and other fucosyltransferases recognize protein substrates with diverse sequences.
Plant biomass provides carbon sources for production of high-value chemical products. Metabolic engineering of a pathway in Escherichia coli that converts pentoses and galacturonate to tricarboxylic acid cycle intermediates provides an efficient route to 1,4-butanediol.
An inducible transcription activator–like effector (TALE) system was developed by inserting tobacco-etch virus (TEV) protease recognition sites into the TALE backbone. The expression of TEV protease degrades the TALE, derepressing plasmid and chromosomal gene expression in Escherichia coli.
The activity of the voltage-sensitive phosphatase from Ciona intestinalis, VSP, towards PIP3 and PIP2 is dictated by the sequential switching between two active conformations of the phosphatase domain that is also correlated with conformational changes in the voltage sensor.
Four secreted bacterial serine hydrolases found by an ABPP approach in Vibrio cholerae–infected rabbits, and one in human infection, regulate the levels of intelectin, an intestinal lectin that binds V. cholerae during infection and may facilitate bacterial surveillance in the intestine.
A high-throughput strategy utilizes a pooled lentiviral approach consisting of a library of 50,000 peptide binding motifs to identify peptide inhibitors of protein-protein interactions that decrease viability in a pancreatic cancer cell line.
Biochemical assays using activity-based chemical probes revealed that the Hippo pathway transcription factor TEAD undergoes autopalmitoylation to ensure binding to YAP/TAZ and promote muscle differentiation and tissue growth.
Laser-based dark field microscopy imaging of a gold-labeled kinesin head during microtubule movement reveals a rightward displacement of unbound kinesin mediated by increased tension in the neck linker.
Lytic polysaccharide monooxygenases (LPMOs) are a class of copper-dependent enzymes that oxidatively degrade polysaccharides and find use in industrial processing of lignocellulose. Crystallographic and spectroscopic studies define how LPMOs recognize their oligosaccharide substrates and mediate oxidative cleavage.
