{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T03:23:56Z","timestamp":1790738636477,"version":"4.1.0"},"reference-count":66,"publisher":"Oxford University Press (OUP)","issue":"5","license":[{"start":{"date-parts":[[2024,2,10]],"date-time":"2024-02-10T00:00:00Z","timestamp":1707523200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2024,3,21]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Environmentally regulated gene expression is critical for bacterial survival under stress conditions, including extremes in temperature, osmolarity and nutrient availability. Here, we dissect the thermo- and osmo-responsory behavior of the transcriptional repressor H-NS, an archetypal nucleoid-condensing sensory protein, ubiquitous in enterobacteria that infect the mammalian gut. Through experiments and thermodynamic modeling, we show that H-NS exhibits osmolarity, temperature and concentration dependent self-association, with a highly polydisperse native ensemble dominated by monomers, dimers, tetramers and octamers. The relative population of these oligomeric states is determined by an interplay between dimerization and higher-order oligomerization, which in turn drives a competition between weak homo- versus hetero-oligomerization of protein-protein and protein-DNA complexes. A phosphomimetic mutation, Y61E, fully eliminates higher-order self-assembly and preserves only dimerization while weakening DNA binding, highlighting that oligomerization is a prerequisite for strong DNA binding. We further demonstrate the presence of long-distance thermodynamic connectivity between dimerization and oligomerization sites on H-NS which influences the binding of the co-repressor Cnu, and switches the DNA binding mode of the hetero-oligomeric H-NS:Cnu complex. Our work thus uncovers important organizational principles in H-NS including a multi-layered thermodynamic control, and provides a molecular framework broadly applicable to other thermo-osmo sensory proteins that employ similar mechanisms to regulate gene expression.<\/jats:p>","DOI":"10.1093\/nar\/gkae090","type":"journal-article","created":{"date-parts":[[2024,1,29]],"date-time":"2024-01-29T07:56:08Z","timestamp":1706514968000},"page":"2157-2173","source":"Crossref","is-referenced-by-count":16,"title":["Molecular and thermodynamic determinants of self-assembly and hetero-oligomerization in the enterobacterial thermo-osmo-regulatory protein H-NS"],"prefix":"10.1093","volume":"52","author":[{"given":"Bincy","family":"Lukose","sequence":"first","affiliation":[{"name":"Department of Biotechnology, Bhupat & Jyoti Mehta School of Biosciences, Indian Institute of Technology Madras , Chennai\u00a0 600036 , India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Takahiro","family":"Maruno","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, Osaka University , Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mohammed\u00a0A","family":"Faidh","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, Bhupat & Jyoti Mehta School of Biosciences, Indian Institute of Technology Madras , Chennai\u00a0 600036 , India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Susumu","family":"Uchiyama","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, Osaka University , Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1655-7802","authenticated-orcid":false,"given":"Athi\u00a0N","family":"Naganathan","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, Bhupat & Jyoti Mehta School of Biosciences, Indian Institute of Technology Madras , Chennai\u00a0 600036 , India"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2024,2,10]]},"reference":[{"key":"2024032102113596500_B1","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1007\/s004380051178","article-title":"Expression of the hemolysin operon in Escherichia Coli is modulated by a nucleoid-protein complex that includes the proteins hha and H-NS","volume":"263","author":"Nieto","year":"2000","journal-title":"Mol. 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