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The heme\u2010based oxygen sensor protein DevS (DosS) plays a key role in this phenomenon, because it is a major activator of the transcription factor DevR. When DevS is active, its histidine protein kinase region is <jats:styled-content style=\"fixed-case\">ON<\/jats:styled-content> and it phosphorylates and activates DevR, which can induce the transcription of the dormancy regulon genes. Here, we have investigated the mechanism by which the ligation of molecular oxygen to a heme\u2010binding domain in DevS switches <jats:styled-content style=\"fixed-case\">OFF<\/jats:styled-content> its histidine protein kinase region. To shed light on the oligomerization states of this protein and possible protein\u2010surfaces of interaction, we used analytical gel filtration, together with dynamic light scattering, fluorescence spectroscopy and chemical crosslinking. We found that DevS exists as three major species: an octamer, a tetramer and a dimer. These three states were observed for the concentration range between 0.5 and 20 \u03bc<jats:sc>m<\/jats:sc> DevS, but not below 0.1 \u03bc<jats:sc>m<\/jats:sc>. Levels of DevS in <jats:italic>M. tuberculosis<\/jats:italic> are expected to range from 5 to 26 \u03bc<jats:sc>m<\/jats:sc>. When this histidine protein kinase was <jats:styled-content style=\"fixed-case\">OFF<\/jats:styled-content>, the DevS was mainly tetrameric and dimeric; by contrast, when the kinase was <jats:styled-content style=\"fixed-case\">ON<\/jats:styled-content>, the protein was predominantly octameric. The changes in quaternary structure were rapid upon binding to the physiological signal. This finding represents a novel strategy for switching the activity of a two\u2010component heme\u2010based sensor. An enhanced understanding of this process might potentially lead to the design of novel regulatory agents that target the multimer interfaces for treatment of latent tuberculosis.<\/jats:p>","DOI":"10.1111\/febs.14734","type":"journal-article","created":{"date-parts":[[2018,12,20]],"date-time":"2018-12-20T11:56:00Z","timestamp":1545306960000},"page":"479-494","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":15,"title":["Oxygen triggers signal transduction in the DevS (DosS) sensor of <i>Mycobacterium tuberculosis<\/i> by modulating the quaternary structure"],"prefix":"10.1111","volume":"286","author":[{"given":"Josiane Bezerra da Silva","family":"Lob\u00e3o","sequence":"first","affiliation":[{"name":"Laboratory of Bioinorganic Chemistry Department of Organic and Inorganic Chemistry Federal University of Ceara Center for Sciences Fortaleza Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ana C. 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