{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,13]],"date-time":"2026-05-13T06:56:09Z","timestamp":1778655369081,"version":"3.51.4"},"reference-count":60,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2014,5,6]],"date-time":"2014-05-06T00:00:00Z","timestamp":1399334400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2014,6]]},"abstract":"Summary<\/jats:title>The environmental bacterium L<\/jats:italic><\/jats:styled-content>egionella pneumophila<\/jats:italic> is the causative agent of Legionnaires' disease, a life\u2010threatening pneumonia. For cell\u2013cell communication the bacteria employ the autoinducer LAI<\/jats:styled-content>\u20101 (3\u2010hydroxypentadecane\u20104\u2010one), which is produced and detected by the Lqs<\/jats:styled-content> (L<\/jats:italic><\/jats:styled-content>egionella<\/jats:italic> quorum sensing) system. The system comprises the autoinducer synthase LqsA<\/jats:styled-content>, the putative sensor kinases LqsS<\/jats:styled-content> and LqsT<\/jats:styled-content>, and the prototypic response regulator LqsR<\/jats:styled-content>. Lqs<\/jats:styled-content>\u2010regulated processes include L<\/jats:italic><\/jats:styled-content>. pneumophila<\/jats:italic>\u2010phagocyte interactions, production of extracellular filaments, and natural competence. Using biochemical approaches we show here that LqsS<\/jats:styled-content> and LqsT<\/jats:styled-content> are autophosphorylated by [\u03b3\u201032<\/jats:sup>P<\/jats:styled-content>]\u2010ATP<\/jats:styled-content> at a conserved histidine residue (H<\/jats:styled-content>200<\/jats:sub> or H<\/jats:styled-content>204<\/jats:sub>) located in their cytoplasmic histidine kinase domain. Pull\u2010down assays revealed that LqsS<\/jats:styled-content> and LqsT<\/jats:styled-content> are bound by LqsR<\/jats:styled-content> or phospho\u2010LqsR<\/jats:styled-content>. Dependent on the conserved receiver domain aspartate (D<\/jats:styled-content>108<\/jats:sub>), the response regulator prevented autophosphorylation of both sensor kinases by catalysing the dephosphorylation of phospho\u2010LqsS<\/jats:styled-content> or phospho\u2010LqsT<\/jats:styled-content>. Moreover, LqsR<\/jats:styled-content> formed dimers upon phosphorylation at D<\/jats:styled-content>108<\/jats:sub> by either acetyl\u2010phosphate or phospho\u2010LqsT<\/jats:styled-content>. Finally, upon heterologous production in E<\/jats:italic><\/jats:styled-content>scherichia coli<\/jats:italic>, LqsT<\/jats:styled-content> (but not LqsS<\/jats:styled-content>) was autophosphorylated by ATP<\/jats:styled-content>, and LqsR<\/jats:styled-content> prevented the autophosphorylation by catalysing the dephosphorylation of phospho\u2010LqsT<\/jats:styled-content>. In summary, these results indicate that phosphorylation signalling through the L<\/jats:italic><\/jats:styled-content>egionella<\/jats:italic> quorum sensing histidine kinases LqsS<\/jats:styled-content> and LqsT<\/jats:styled-content> converges on the response regulator LqsR<\/jats:styled-content>.<\/jats:p>","DOI":"10.1111\/mmi.12612","type":"journal-article","created":{"date-parts":[[2014,4,11]],"date-time":"2014-04-11T06:50:49Z","timestamp":1397199049000},"page":"1039-1055","source":"Crossref","is-referenced-by-count":34,"title":["Phosphorylation signalling through the L<\/i><\/scp>egionella<\/i> quorum sensing histidine kinases LqsS<\/scp> and LqsT<\/scp> converges on the response regulator LqsR<\/scp>"],"prefix":"10.1111","volume":"92","author":[{"given":"Ursula","family":"Schell","sequence":"first","affiliation":[{"name":"Max von Pettenkofer Institute Ludwig\u2010Maximilians University Pettenkoferstra\u00dfe 9a 80336 Munich 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