ArticlebioRxiv : the preprint server for biology2025
A Pipeline for Screening Small Molecule-Enhanced Protein Stability in A Bacterial Orphan Receptor.
Article in bioRxiv : the preprint server for biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Bacterial one-component signaling proteins integrate sensory and gene regulation functions within the same polypeptide, creating powerful natural sensors of environmental conditions which can also be adapted into powerful tools for synthetic biology and biotechnology. A key sensor motif within many of these proteins is the Per-ARNT-Sim (PAS) domain, known for its conserved fold yet highly divergent sequences, allowing for a broad range of ligands to control PAS protein function by changes in small molecule binding occupancy or configuration. This diversity introduces a challenging step - identification of ligands for "orphan" PAS proteins which show signatures of ligand binding but no copurifying high-affinity bound small molecules - into characterization and engineering of such proteins. In this study, we characterized CU228, a putative PAS-HTH transcription factor from
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