Biology subjects

Pohl, R.

Publications and source records attributed to Pohl, R..

3 recordsLinked to original sources

bioRxiv2026

ChemCell: Chemical Tethering of Large Biomolecules to Cell Surfaces through Diels-Alder Ligation

Chemical engineering of cellular surfaces offers a powerful tool to endow cells with new properties and functions, yet methods for adding complex biomolecules to cell membranes remain underdeveloped. While technologies for targeted degradation of cell surface components are advancing, few approaches exist that allow efficient attachment of large biomolecules. To address this, we introduce ChemCell technology--a platform for non-genetic surface engineering of cells via metabolic installation of trans-cyclooctene (TCO) groups. These TCO groups undergo rapid and selective reactions with tetrazine-modified biomolecules, enabling the efficient tethering of diverse functional groups. This method allows for the precise attachment of proteins, peptides, enzymes, oligonucleotides, therapeutic antibodies, and large protein complexes to cell surfaces, expanding the toolbox for cellular modification and offering new possibilities for cell-based therapies and diagnostics.

biochemistry↗

bioRxiv2026

Evolutionary origin of terpenoid biosynthesis in termites

Termites produce the most diverse array of terpenoids among metazoans, comprising over 200 structures. However, their biosynthesis has not yet been elucidated. Here, we identify a gene family which arose through the duplication of geranylgeranyl pyrophosphate synthase in the common ancestor of Neoisoptera, the terpene-producing termite lineage. We functionally characterized several proteins from this family as terpene synthases generating biologically relevant sesqui-and diterpenes. These include the queen pheromone (3R,6E)-nerolidol in Embiratermes neotenicus and the precursor of polycyclic defensive diterpenes (E,E,E)-neocembrene in Nasutitermes takasagoensis. We explore transposable element-mediated genomic mechanisms and selection pressures acting in the evolution of this gene family and report an amino acid site crucial for cyclization capacity as well as the enantiospecificity of the characterized enzymes. We conclude that we have identified an enzyme family underlying the remarkable richness of termite terpenoids, which likely contributed to the ecological success of Neoisoptera.

biochemistry↗

bioRxiv2021

RelA-SpoT Homologue toxins pyrophosphorylate the CCA end of tRNA to inhibit protein synthesis

RelA-SpoT Homolog (RSH) enzymes control bacterial physiology through synthesis and degradation of the nucleotide alarmone (p)ppGpp. We recently discovered multiple families of Small Alarmone Synthetase (SAS) RSH acting as toxins of toxin-antitoxin (TA) modules, with the FaRel subfamily of toxSAS abrogating bacterial growth by producing an analogue of (p)ppGpp, (pp)pApp. Here we probe the mechanism of growth arrest employed by four experimentally unexplored subfamilies of toxSAS: FaRel2, PhRel, PhRel2 and CapRel. Surprisingly, all these toxins specifically inhibit protein synthesis. To do so, they transfer a pyrophosphate moiety from ATP to the tRNA 3' CCA. The modification inhibits both tRNA aminoacylation and the sensing of cellular amino acid starvation by the ribosome-associated RSH RelA. Conversely, we show that some Small Alarmone Hydrolase (SAH) RSH enzymes can reverse the pyrophosphorylation of tRNA to counter the growth inhibition by toxSAS. Collectively, we establish RSHs as a novel class of RNA-modifying enzymes.

microbiology↗