{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zheng CR"],"funding":["Intelligence Advanced Research Projects Activity","Army Research Office","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["2340-2350"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8498941"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(9)"],"pubmed_abstract":["At the single-cell level, protein kinase activity is typically inferred from downstream transcriptional reporters. However, promoters are often coregulated by several pathways, making the activity of a specific kinase difficult to deconvolve. Here, we present modular, direct, and specific sensors of bacterial kinase activity, including FRET-based sensors, as well as a synthetic transcription factor based on the lactose repressor (LacI) that has been engineered to respond to phosphorylation. We demonstrate the utility of these sensors in measuring the activity of PrkC, a conserved bacterial Ser/Thr kinase, in different growth conditions from single cells to colonies. We also show that PrkC activity increases in response to a cell-wall active antibiotic that blocks the late steps in peptidog"],"journal":["ACS synthetic biology"],"pubmed_title":["Modular and Single-Cell Sensors of Bacterial Ser/Thr Kinase Activity."],"pmcid":["PMC8498941"],"funding_grant_id":["N660011824505","W911NF1910243","R01GM124446","R01 GM124446"],"pubmed_authors":["Libby A","Zheng CR","Singh A","Silver PA","Libby EA"],"additional_accession":[]},"is_claimable":false,"name":"Modular and Single-Cell Sensors of Bacterial Ser/Thr Kinase Activity.","description":"At the single-cell level, protein kinase activity is typically inferred from downstream transcriptional reporters. However, promoters are often coregulated by several pathways, making the activity of a specific kinase difficult to deconvolve. Here, we present modular, direct, and specific sensors of bacterial kinase activity, including FRET-based sensors, as well as a synthetic transcription factor based on the lactose repressor (LacI) that has been engineered to respond to phosphorylation. We demonstrate the utility of these sensors in measuring the activity of PrkC, a conserved bacterial Ser/Thr kinase, in different growth conditions from single cells to colonies. We also show that PrkC activity increases in response to a cell-wall active antibiotic that blocks the late steps in peptidog","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Sep","modification":"2025-04-26T16:31:51.313Z","creation":"2025-02-19T00:47:39.912Z"},"accession":"S-EPMC8498941","cross_references":{"pubmed":["34463482"],"doi":["10.1021/acssynbio.1c00250"]}}