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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.

    • Yinjie J. Tang
    • Tae Seok Moon
    News & Views
  • 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.

    • Paulo Onuchic
    • Steven Boeynaems
    News & Views
  • 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.

    Research Briefing
  • 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.

    • A. Nikolai von Krusenstiern
    • Ryan N. Robson
    • Brent R. Stockwell
    Article
  • 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.

    • Rebecca A. Wilkes
    • Jacob Waldbauer
    • Ludmilla Aristilde
    Article Open Access
  • 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.

    • Yifan Dai
    • Mina Farag
    • Lingchong You
    Article
  • 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.

    • Brandán Pedre
    • Deepti Talwar
    • Tobias P. Dick
    Article Open Access
  • 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.

    Research Briefing
  • 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.

    • Tung T. Le
    • Meiling Wu
    • Michelle D. Wang
    Article Open Access
  • 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.

    • Danielle A. Yee
    • Kanji Niwa
    • Yi Tang
    Article
  • 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.

    • Giorgio Caserta
    • Sven Hartmann
    • Oliver Lenz
    Article
  • 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.

    • Marion Jespersen
    • Antonio J. Pierik
    • Tristan Wagner
    Article Open Access