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Comamonas testosteroni utilizes aromatic compounds such as monomers from lignin and plastics, but the underlying metabolic pathways were elusive. Multi-omics analysis now clarifies the multifaceted regulation of its metabolism, facilitating strain engineering to convert substrates from lignin and plastics into valuable bioproducts.
A modular platform was developed to generate designer condensates with tunable material properties for selective partitioning. These programmable assemblies can regulate bacterial plasmid expression and inheritance but will find a broad array of applications, including in eukaryote systems.
Ferroptosis can be induced by lipid peroxidation in various subcellular membranes, including the endoplasmic reticulum (ER), mitochondria and lysosomes. By studying the subcellular distribution of ferroptosis-modulating fatty acids, we observed that the ER is a key initial site of peroxidation, followed by the plasma membrane, whereas other organelles are not as critical for ferroptosis.
Ferroptosis is a lipid-peroxide-driven cell death with promising therapeutic applications. Although peroxidation of various subcellular membranes can initiate ferroptosis, the authors found that the endoplasmic reticulum is an essential site.
Aromatic carbon fluxes for the metabolism of lignin and plastics derivatives in Comamonas testosteroni KF-1 are controlled by pathway-specific regulation at transcript, protein or metabolite levels. The combination of transcriptional activation and metabolic fine-tuning complicates predictions of modulated carbon and energy fluxes during metabolic engineering strategies.
Dai et al. present a streamlined approach for the design and engineering of synthetic biomolecular condensates for controlling different cellular processes, such as gene flow, transcriptional regulation and modulation of protein circuits.
Mercaptopyruvate sulfur transferase (MPST) is revealed as a protein persulfidase that acts directly on numerous and diverse target proteins, revealing potential origins of persulfidation as a common posttranslational modification.
A potent and selective degrader was developed that depletes STAT5 in cells and mouse tissues, exerts cell growth inhibition in cells with activated STAT5 and induces tumor regression in mouse models.
Etoposide, a chemotherapeutic poison of type IIA eukaryotic topoisomerases (topo IIs), promotes topo II to compact DNA by trapping DNA loops, creates DNA double-strand breaks, causes topo II to resist relocation, and pauses the ability of topoisomerases to relax DNA supercoiling. Through these mechanisms, etoposide converts topo II into a roadblock to DNA processing.
Using single-molecule biophysics methods, Le et al. discovered that etoposide, a chemotherapeutic poison of topoisomerase II (topo II), promotes topo II to compact DNA, trap DNA loops and pause DNA supercoiling relaxation, thus converting topo II into a strong roadblock to DNA processing.
A new biosynthetic core-forming enzyme, arginine cyclodipeptide synthase (RCDPS), was found to produce cyclo-arginine-Xaa dipeptides via a tRNA-dependent mechanism, and further genome mining using RCDPS as a beacon uncovered new natural products.
The multistep incorporation process of the catalytic NiFe(CN)2(CO) cofactor into [NiFe]-hydrogenase was deciphered by isolating key maturation intermediates, which were characterized by biochemical and a variety of spectroscopic techniques.
A bifunctional amino acid, photo-ANA, equipped with a bio-orthogonal handle and a photoreactive warhead, specifically labels Salmonella spp. during infection and enables the profiling of proteome dynamics and host–pathogen protein–protein interactions.
The F420-dependent sulfite reductase protects some methanogenic archaea by converting toxic sulfite. Structural analysis reveals how the two active centers are electro-connected and provides a plausible picture of a primitive sulfite reductase.
