{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,6]],"date-time":"2026-09-06T04:28:58Z","timestamp":1788668938959,"version":"build-2803163510"},"reference-count":57,"publisher":"Wiley","license":[{"start":{"date-parts":[[2026,6,16]],"date-time":"2026-06-16T00:00:00Z","timestamp":1781568000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,6,16]],"date-time":"2026-06-16T00:00:00Z","timestamp":1781568000000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R35GM131760"],"award-info":[{"award-number":["R35GM131760"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000054","name":"National Cancer Institute","doi-asserted-by":"publisher","award":["P30CA008748"],"award-info":[{"award-number":["P30CA008748"]}],"id":[{"id":"10.13039\/100000054","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["R01AI138446"],"award-info":[{"award-number":["R01AI138446"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"abstract":"<jats:p>\n                    Two\u2010component systems (TCS) mediate bacterial signal transduction in response to specific environmental conditions. The two components are the sensor kinase (SK), which senses the signal and autophosphorylates on a histidine residue, and a response regulator (RR), which is phosphorylated by the kinase and modifies gene expression. Despite intensive study, the mechanisms of signal sensing by sensor kinases remain incompletely defined, and it is yet unclear how these kinases sense multiple ligands.\n                    <jats:italic>Mycobacterium tuberculosis<\/jats:italic>\n                    PdtaS\/PdtaR is a soluble TCS pair that participates in the Rip1 signal transduction cascade to control virulence by responding to copper and nitric oxide (NO). In contrast to paradigmatic ligand\u2010activated SKs, PdtaS is constitutively active in the absence of a ligand and is directly inhibited by Cu or NO, yet it remains unclear how such chemically diverse ligands are sensed. Here, we show that PdtaS is a dimeric kinase that constitutively autophosphorylates in\n                    <jats:italic>trans<\/jats:italic>\n                    . Cu and NO both inhibit PdtaS phosphorylation by inhibiting dimerization. Phylogenetic analysis of the PdtaS family reveals conservation of the GAF\/PAS dimer interface rather than the ligand\u2010binding pockets. Mutations in the GAF dimer interface that alter dimerization impair multi\u2010ligand sensing both\n                    <jats:italic>in vitro<\/jats:italic>\n                    and in\n                    <jats:italic>M. tuberculosis<\/jats:italic>\n                    cells. These results indicate that a single bacterial kinase can sense chemically diverse inputs through inhibition of dimerization\u2010dependent phosphorylation.\n                  <\/jats:p>","DOI":"10.1111\/febs.70621","type":"journal-article","created":{"date-parts":[[2026,6,17]],"date-time":"2026-06-17T05:16:37Z","timestamp":1781673397000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Ligand binding represses bacterial histidine kinase activity by inhibiting its dimerization"],"prefix":"10.1111","author":[{"given":"Gaurav D.","family":"Sankhe","sequence":"first","affiliation":[{"name":"Immunology Program Sloan Kettering Institute  New York New York USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jiawei","family":"Xing","sequence":"additional","affiliation":[{"name":"Department of Microbiology The Ohio State University  Columbus OH 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