{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T20:29:52Z","timestamp":1792700992717,"version":"4.5.0"},"reference-count":76,"publisher":"Oxford University Press (OUP)","issue":"4","license":[{"start":{"date-parts":[[2020,1,11]],"date-time":"2020-01-11T00:00:00Z","timestamp":1578700800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"funder":[{"name":"Netherlands Organization for Scientific Research","award":["VICI 016.160.613"],"award-info":[{"award-number":["VICI 016.160.613"]}]},{"DOI":"10.13039\/501100000854","name":"Human Frontier Science Program","doi-asserted-by":"publisher","award":["RGP0014\/2014"],"award-info":[{"award-number":["RGP0014\/2014"]}],"id":[{"id":"10.13039\/501100000854","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004543","name":"China Scholarship Council","doi-asserted-by":"publisher","award":["201506880001"],"award-info":[{"award-number":["201506880001"]}],"id":[{"id":"10.13039\/501100004543","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2020,2,28]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>H-NS proteins act as osmotic sensors translating changes in osmolarity into altered DNA binding properties, thus, regulating enterobacterial genome organization and genes transcription. The molecular mechanism underlying the switching process and its conservation among H-NS family members remains elusive. Here, we focus on the H-NS family protein MvaT from Pseudomonas aeruginosa and demonstrate experimentally that its protomer exists in two different conformations, corresponding to two different functional states. In the half-opened state (dominant at low salt) the protein forms filaments along DNA, in the fully opened state (dominant at high salt) the protein bridges DNA. This switching is a direct effect of ionic strength on electrostatic interactions between the oppositely charged DNA binding and N-terminal domains of MvaT. The asymmetric charge distribution and intramolecular interactions are conserved among the H-NS family of proteins. Therefore, our study establishes a general paradigm for the molecular mechanistic basis of the osmosensitivity of H-NS proteins.<\/jats:p>","DOI":"10.1093\/nar\/gkz1226","type":"journal-article","created":{"date-parts":[[2019,12,19]],"date-time":"2019-12-19T23:37:26Z","timestamp":1576798646000},"page":"2156-2172","source":"Crossref","is-referenced-by-count":46,"title":["Structural basis for osmotic regulation of the DNA binding properties of H-NS proteins"],"prefix":"10.1093","volume":"48","author":[{"given":"Liang","family":"Qin","sequence":"first","affiliation":[{"name":"Department of Macromolecular Biochemistry, Leiden Institute of Chemistry, Einsteinweg 55, 2333 CC Leiden, the Netherlands"},{"name":"Centre for Microbial Cell Biology, Leiden University, Einsteinweg 55, 2333CC Leiden, the Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fredj Ben","family":"Bdira","sequence":"first","affiliation":[{"name":"Department of Macromolecular Biochemistry, Leiden Institute of Chemistry, Einsteinweg 55, 2333 CC Leiden, the Netherlands"},{"name":"Centre for Microbial Cell Biology, Leiden University, Einsteinweg 55, 2333CC Leiden, the Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yann G J","family":"Sterckx","sequence":"first","affiliation":[{"name":"Laboratory of Medical Biochemistry, University of Antwerp, Campus Drie Eiken, University Square 1, 2610 Wilrijk, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexander N","family":"Volkov","sequence":"first","affiliation":[{"name":"VIB-VUB Structural Biology Research Center, Pleinlaan 2, 1050 Brussels, Belgium"},{"name":"Jean Jeener NMR Centre, VUB, Pleinlaan 2, 1050 Brussels, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jocelyne","family":"Vreede","sequence":"first","affiliation":[{"name":"Department of Computational Chemistry, Van\u2019t Hoff Institute for Molecular Sciences, University of Amsterdam Science Park 904, 1098 XH Amsterdam, the Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gabriele","family":"Giachin","sequence":"first","affiliation":[{"name":"Structural Biology Group, European Synchrotron Radiation Facility (ESRF), Grenoble, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter","family":"van\u00a0Schaik","sequence":"first","affiliation":[{"name":"Department of Macromolecular Biochemistry, Leiden Institute of Chemistry, Einsteinweg 55, 2333 CC Leiden, the Netherlands"},{"name":"Centre for Microbial Cell Biology, Leiden University, Einsteinweg 55, 2333CC Leiden, the Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marcellus","family":"Ubbink","sequence":"first","affiliation":[{"name":"Department of Macromolecular Biochemistry, Leiden Institute of Chemistry, Einsteinweg 55, 2333 CC Leiden, the Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Remus\u00a0T","family":"Dame","sequence":"first","affiliation":[{"name":"Department of Macromolecular Biochemistry, Leiden Institute of Chemistry, Einsteinweg 55, 2333 CC Leiden, the Netherlands"},{"name":"Centre for Microbial Cell Biology, Leiden University, Einsteinweg 55, 2333CC Leiden, the Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2020,1,11]]},"reference":[{"key":"2020022408400831700_B1","doi-asserted-by":"crossref","first-page":"544","DOI":"10.1002\/wsbm.136","article-title":"Adaptation of cells to new environments","volume":"3","author":"Brooks","year":"2011","journal-title":"Wiley Interdiscip. Rev. Syst. Biol. Med."},{"key":"2020022408400831700_B2","doi-asserted-by":"crossref","first-page":"2019","DOI":"10.3389\/fmicb.2018.02019","article-title":"Impact of chromosomal architecture on the function and evolution of bacterial genomes","volume":"9","author":"Krogh","year":"2018","journal-title":"Front. Microbiol."},{"key":"2020022408400831700_B3","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1038\/nrmicro883","article-title":"H-NS: a universal regulator for a dynamic genome","volume":"2","author":"Dorman","year":"2004","journal-title":"Nat. Rev. Microbiol."},{"key":"2020022408400831700_B4","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1016\/j.tim.2003.09.005","article-title":"H-NS in Gram-negative bacteria: a family of multifaceted proteins","volume":"11","author":"Tendeng","year":"2003","journal-title":"Trends Microbiol."},{"key":"2020022408400831700_B5","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1046\/j.1365-2958.1997.3151679.x","article-title":"H-NS: a modulator of environmentally regulated gene expression","volume":"24","author":"Atlung","year":"1997","journal-title":"Mol. Microbiol."},{"key":"2020022408400831700_B6","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1046\/j.1365-2958.1998.01049.x","article-title":"Temperature sensing in bacterial gene regulation\u2014what it all boils down to","volume":"30","author":"Hurme","year":"1998","journal-title":"Mol. Microbiol."},{"key":"2020022408400831700_B7","doi-asserted-by":"crossref","first-page":"190223","DOI":"10.1098\/rsob.190223","article-title":"The architects of bacterial DNA bridges: a structurally and functionally conserved family of proteins","volume":"9","author":"Qin","year":"2019","journal-title":"Open Biol."},{"key":"2020022408400831700_B8","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/j.mib.2011.12.014","article-title":"Silencing of foreign DNA in bacteria","volume":"15","author":"Ali","year":"2012","journal-title":"Curr. Opin. Microbiol."},{"key":"2020022408400831700_B9","doi-asserted-by":"crossref","first-page":"1456","DOI":"10.1101\/gad.1543107","article-title":"Silencing of xenogeneic DNA by H-NS\u2014facilitation of lateral gene transfer in bacteria by a defense system that recognizes foreign DNA","volume":"21","author":"Navarre","year":"2007","journal-title":"Genes Dev."},{"key":"2020022408400831700_B10","doi-asserted-by":"crossref","first-page":"e81","DOI":"10.1371\/journal.ppat.0020081","article-title":"H-NS mediates the silencing of laterally acquired genes in bacteria","volume":"2","author":"Lucchini","year":"2006","journal-title":"PLoS Pathog."},{"key":"2020022408400831700_B11","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1126\/science.1128794","article-title":"Selective silencing of foreign DNA with low GC content by the H-NS protein in Salmonella","volume":"313","author":"Navarre","year":"2006","journal-title":"Science"},{"key":"2020022408400831700_B12","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1101\/gad.234336.113","article-title":"Widespread suppression of intragenic transcription initiation by H-NS","volume":"28","author":"Singh","year":"2014","journal-title":"Genes Dev."},{"key":"2020022408400831700_B13","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1093\/dnares\/dsl009","article-title":"Escherichia coli histone-like protein H-NS preferentially binds to horizontally acquired DNA in association with RNA polymerase","volume":"13","author":"Oshima","year":"2006","journal-title":"DNA res."},{"key":"2020022408400831700_B14","doi-asserted-by":"crossref","first-page":"10690","DOI":"10.1073\/pnas.1102544108","article-title":"Structural basis for recognition of AT-rich DNA by unrelated xenogeneic silencing proteins","volume":"108","author":"Gordon","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2020022408400831700_B15","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1038\/nsmb1233","article-title":"H-NS cooperative binding to high-affinity sites in a regulatory element results in transcriptional silencing","volume":"14","author":"Bouffartigues","year":"2007","journal-title":"Nat. Struct. Mol. Biol."},{"key":"2020022408400831700_B16","doi-asserted-by":"crossref","first-page":"1311","DOI":"10.1046\/j.1365-2958.2001.02706.x","article-title":"A molecular mechanism for the repression of transcription by the H-NS protein","volume":"42","author":"Rimsky","year":"2001","journal-title":"Mol. Microbiol."},{"key":"2020022408400831700_B17","doi-asserted-by":"crossref","first-page":"2467","DOI":"10.1016\/S0006-3495(03)75051-6","article-title":"Increased bending rigidity of single DNA molecules by H-NS, a temperature and osmolarity sensor","volume":"84","author":"Amit","year":"2003","journal-title":"Biophys. J."},{"key":"2020022408400831700_B18","doi-asserted-by":"crossref","first-page":"R913","DOI":"10.1016\/j.cub.2007.09.005","article-title":"H-NS promotes looped domain formation in the bacterial chromosome","volume":"17","author":"Noom","year":"2007","journal-title":"Curr. Biol."},{"key":"2020022408400831700_B19","doi-asserted-by":"crossref","first-page":"1845","DOI":"10.1128\/JB.187.5.1845-1848.2005","article-title":"DNA bridging: a property shared among H-NS-like proteins","volume":"187","author":"Dame","year":"2005","journal-title":"J. Bacteriol."},{"key":"2020022408400831700_B20","doi-asserted-by":"crossref","first-page":"e27369","DOI":"10.7554\/eLife.27369","article-title":"Mechanism of environmentally driven conformational changes that modulate H-NS DNA-bridging activity","volume":"6","author":"van\u00a0der\u00a0Valk","year":"2017","journal-title":"Elife"},{"key":"2020022408400831700_B21","doi-asserted-by":"crossref","first-page":"2146","DOI":"10.1074\/jbc.C100603200","article-title":"Structural basis for H-NS-mediated trapping of RNA polymerase in the open initiation complex at the rrnB P1","volume":"277","author":"Dame","year":"2002","journal-title":"J. Biol. Chem."},{"key":"2020022408400831700_B22","doi-asserted-by":"crossref","first-page":"3504","DOI":"10.1093\/nar\/28.18.3504","article-title":"H-NS mediated compaction of DNA visualised by atomic force microscopy","volume":"28","author":"Dame","year":"2000","journal-title":"Nucleic Acids Res."},{"key":"2020022408400831700_B23","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1101\/gad.1883510","article-title":"A divalent switch drives H-NS\/DNA-binding conformations between stiffening and bridging modes","volume":"24","author":"Liu","year":"2010","journal-title":"Genes Dev."},{"key":"2020022408400831700_B24","doi-asserted-by":"crossref","first-page":"1321","DOI":"10.1016\/j.bpj.2015.08.016","article-title":"H-NS regulates gene expression and compacts the nucleoid: insights from single-molecule experiments","volume":"109","author":"Winardhi","year":"2015","journal-title":"Biophys. J."},{"key":"2020022408400831700_B25","doi-asserted-by":"crossref","first-page":"2666","DOI":"10.1093\/nar\/gky1299","article-title":"H-NS uses an autoinhibitory conformational switch for environment-controlled gene silencing","volume":"47","author":"Shahul\u00a0Hameed","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"2020022408400831700_B26","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1016\/S0966-842X(99)01455-9","article-title":"Domain organization and oligomerization among H-NS-like nucleoid-associated proteins in bacteria","volume":"7","author":"Dorman","year":"1999","journal-title":"Trends Microbiol."},{"key":"2020022408400831700_B27","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/j.mib.2004.02.001","article-title":"Structure of the histone-like protein H-NS and its role in regulation and genome superstructure","volume":"7","author":"Rimsky","year":"2004","journal-title":"Curr. Opin. Microbiol."},{"key":"2020022408400831700_B28","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1111\/j.1365-2958.2009.06754.x","article-title":"Investigation of the self-association and hetero-association interactions of H-NS and StpA from Enterobacteria","volume":"73","author":"Leonard","year":"2009","journal-title":"Mol. Microbiol."},{"key":"2020022408400831700_B29","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/0014-5793(95)00079-O","article-title":"Solution structure of the DNA binding domain of a nucleoid-associated protein, H-NS, from Escherichia coli","volume":"360","author":"Shindo","year":"1995","journal-title":"FEBS lett."},{"key":"2020022408400831700_B30","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1016\/S0022-2836(02)01141-5","article-title":"H-NS oligomerization domain structure reveals the mechanism for high order self-association of the intact protein","volume":"324","author":"Esposito","year":"2002","journal-title":"J. Mol. Biol."},{"key":"2020022408400831700_B31","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1038\/nsb904","article-title":"The H-NS dimerization domain defines a new fold contributing to DNA recognition","volume":"10","author":"Bloch","year":"2003","journal-title":"Nat. Struct. Mol. Biol."},{"key":"2020022408400831700_B32","doi-asserted-by":"crossref","first-page":"15728","DOI":"10.1073\/pnas.1006966107","article-title":"H-NS forms a superhelical protein scaffold for DNA condensation","volume":"107","author":"Arold","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2020022408400831700_B33","doi-asserted-by":"crossref","first-page":"962","DOI":"10.1046\/j.1365-2958.2000.01917.x","article-title":"Oligomerization of the chromatin-structuring protein H-NS","volume":"36","author":"Smyth","year":"2000","journal-title":"Mol. Microbiol."},{"key":"2020022408400831700_B34","doi-asserted-by":"crossref","first-page":"2916","DOI":"10.1111\/febs.12297","article-title":"Protein oligomers studied by solid-state NMR\u2013the case of the full-length nucleoid-associated protein histone-like nucleoid structuring protein","volume":"280","author":"Renault","year":"2013","journal-title":"FEBS J."},{"key":"2020022408400831700_B35","doi-asserted-by":"crossref","first-page":"3797","DOI":"10.1099\/mic.0.27270-0","article-title":"The Pseudomonas aeruginosa global regulator MvaT specifically binds to the ptxS upstream region and enhances ptxS expression","volume":"150","author":"Westfall","year":"2004","journal-title":"Microbiology"},{"key":"2020022408400831700_B36","doi-asserted-by":"crossref","first-page":"2880","DOI":"10.1128\/JB.186.9.2880-2890.2004","article-title":"Biofilm formation in Pseudomonas aeruginosa: fimbrial cup gene clusters are controlled by the transcriptional regulator MvaT","volume":"186","author":"Vallet","year":"2004","journal-title":"J. Bacteriol."},{"key":"2020022408400831700_B37","doi-asserted-by":"crossref","first-page":"18947","DOI":"10.1073\/pnas.0808215105","article-title":"H-NS family members function coordinately in an opportunistic pathogen","volume":"105","author":"Castang","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2020022408400831700_B38","doi-asserted-by":"crossref","first-page":"916","DOI":"10.1111\/j.1365-2958.2010.07378.x","article-title":"High-order oligomerization is required for the function of the H-NS family member MvaT in Pseudomonas aeruginosa","volume":"78","author":"Castang","year":"2010","journal-title":"Mol. Microbiol."},{"key":"2020022408400831700_B39","doi-asserted-by":"crossref","first-page":"8942","DOI":"10.1093\/nar\/gks669","article-title":"Higher order oligomerization is required for H-NS family member MvaT to form gene-silencing nucleoprotein filament","volume":"40","author":"Winardhi","year":"2012","journal-title":"Nucleic Acids Res."},{"key":"2020022408400831700_B40","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1038\/nmeth.1318","article-title":"Enzymatic assembly of DNA molecules up to several hundred kilobases","volume":"6","author":"Gibson","year":"2009","journal-title":"Nat. Methods"},{"key":"2020022408400831700_B41","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1007\/978-1-4939-7098-8_11","volume-title":"The Bacterial Nucleoid: Methods and Protocols","author":"van\u00a0der\u00a0Valk","year":"2017"},{"key":"2020022408400831700_B42","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1007\/978-1-4939-8675-0_12","volume-title":"Bacterial Chromatin","author":"van\u00a0der\u00a0Valk","year":"2018"},{"key":"2020022408400831700_B43","doi-asserted-by":"crossref","first-page":"660","DOI":"10.1107\/S0909049513010431","article-title":"Upgraded ESRF BM29 beamline for SAXS on macromolecules in solution","volume":"20","author":"Pernot","year":"2013","journal-title":"Synchrotron Radiat."},{"key":"2020022408400831700_B44","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1107\/S0021889899015216","article-title":"SAXS experiments on absolute scale with Kratky systems using water as a secondary standard","volume":"33","author":"Orthaber","year":"2000","journal-title":"J. Appl. Crystallogr."},{"key":"2020022408400831700_B45","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1107\/S1600576715024462","article-title":"Online data analysis at the ESRF bioSAXS beamline, BM29","volume":"49","author":"Brennich","year":"2016","journal-title":"J. Appl. Crystallogr."},{"key":"2020022408400831700_B46","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1107\/S0021889812007662","article-title":"New developments in the ATSAS program package for small-angle scattering data analysis","volume":"45","author":"Petoukhov","year":"2012","journal-title":"J. Appl. Crystallogr."},{"key":"2020022408400831700_B47","doi-asserted-by":"crossref","first-page":"1212","DOI":"10.1107\/S1600576717007786","article-title":"ATSAS 2.8: a comprehensive data analysis suite for small-angle scattering from macromolecular solutions","volume":"50","author":"Franke","year":"2017","journal-title":"J. Appl. Crystallogr."},{"key":"2020022408400831700_B48","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1107\/S0021889892001663","article-title":"Determination of the regularization parameter in indirect-transform methods using perceptual criteria","volume":"25","author":"Svergun","year":"1992","journal-title":"J. Appl. Crystallogr."},{"key":"2020022408400831700_B49","doi-asserted-by":"crossref","first-page":"1325","DOI":"10.1093\/bioinformatics\/btu830","article-title":"NMRFAM-SPARKY: enhanced software for biomolecular NMR spectroscopy","volume":"31","author":"Lee","year":"2014","journal-title":"Bioinformatics"},{"key":"2020022408400831700_B50","doi-asserted-by":"crossref","first-page":"687","DOI":"10.1002\/prot.20449","article-title":"The CCPN data model for NMR spectroscopy: development of a software pipeline","volume":"59","author":"Vranken","year":"2005","journal-title":"Proteins."},{"key":"2020022408400831700_B51","doi-asserted-by":"crossref","first-page":"24826","DOI":"10.1038\/srep24826","article-title":"Two-dimensional NMR lineshape analysis","volume":"6","author":"Waudby","year":"2016","journal-title":"Sci. Rep."},{"key":"2020022408400831700_B52","doi-asserted-by":"crossref","first-page":"5355","DOI":"10.1021\/bi000060h","article-title":"Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data","volume":"39","author":"Battiste","year":"2000","journal-title":"Biochemistry"},{"key":"2020022408400831700_B53","doi-asserted-by":"crossref","first-page":"e1004967","DOI":"10.1371\/journal.ppat.1004967","article-title":"A novel AT-rich DNA recognition mechanism for bacterial xenogeneic silencer MvaT","volume":"11","author":"Ding","year":"2015","journal-title":"PLoS Pathog."},{"key":"2020022408400831700_B54","doi-asserted-by":"crossref","first-page":"3583","DOI":"10.1002\/1873-3468.12425","article-title":"Structural similarities and differences in H-NS family proteins revealed by the N-terminal structure of TurB in Pseudomonas putida KT2440","volume":"590","author":"Suzuki-Minakuchi","year":"2016","journal-title":"FEBS Lett."},{"key":"2020022408400831700_B55","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/S1090-7807(02)00014-9","article-title":"The Xplor-NIH NMR molecular structure determination package","volume":"160","author":"Schwieters","year":"2003","journal-title":"J. Magn. Reson."},{"key":"2020022408400831700_B56","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.pnmrs.2005.10.001","article-title":"Using Xplor\u2013NIH for NMR molecular structure determination","volume":"48","author":"Schwieters","year":"2006","journal-title":"Prog. Nucl. Magn. Reson. Spectrosc."},{"key":"2020022408400831700_B57","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.pnmrs.2014.03.001","article-title":"Using small angle solution scattering data in Xplor-NIH structure calculations","volume":"80","author":"Schwieters","year":"2014","journal-title":"Prog. Nucl. Magn. Reson. Spectrosc."},{"key":"2020022408400831700_B58","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1002\/pro.3248","article-title":"Xplor-NIH for molecular structure determination from NMR and other data sources","volume":"27","author":"Schwieters","year":"2018","journal-title":"Protein Sci."},{"key":"2020022408400831700_B59","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1038\/nature05201","article-title":"Visualization of transient encounter complexes in protein\u2013protein association","volume":"444","author":"Tang","year":"2006","journal-title":"Nature"},{"key":"2020022408400831700_B60","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF Chimera\u2014a visualization system for exploratory research and analysis","volume":"25","author":"Pettersen","year":"2004","journal-title":"J. Comput. Chem."},{"key":"2020022408400831700_B61","doi-asserted-by":"crossref","first-page":"12560","DOI":"10.1073\/pnas.1716721114","article-title":"Charged residues in the H-NS linker drive DNA binding and gene silencing in single cells","volume":"114","author":"Gao","year":"2017","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2020022408400831700_B62","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/S0014-5793(99)00862-5","article-title":"Identification of the DNA binding surface of H-NS protein from Escherichia coli by heteronuclear NMR spectroscopy","volume":"455","author":"Shindo","year":"1999","journal-title":"FEBS Lett."},{"key":"2020022408400831700_B63","doi-asserted-by":"crossref","first-page":"2347","DOI":"10.1016\/j.jmb.2013.03.006","article-title":"On the origin of the selectivity of plasmidic H-NS towards horizontally acquired DNA: linking H-NS oligomerization and cooperative DNA binding","volume":"425","author":"Fern\u00e1ndez-de-Alba","year":"2013","journal-title":"J. Mol. Biol."},{"key":"2020022408400831700_B64","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1093\/nar\/gky497","article-title":"BeStSel: a web server for accurate protein secondary structure prediction and fold recognition from the circular dichroism spectra","volume":"46","author":"Micsonai","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"2020022408400831700_B65","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1007\/s10858-005-5705-1","article-title":"Protein energetic conformational analysis from NMR chemical shifts (PECAN) and its use in determining secondary structural elements","volume":"32","author":"Eghbalnia","year":"2005","journal-title":"J. Biomol. NMR."},{"key":"2020022408400831700_B66","doi-asserted-by":"crossref","first-page":"4108","DOI":"10.1021\/cr900033p","article-title":"Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes","volume":"109","author":"Clore","year":"2009","journal-title":"Chem. Rev."},{"key":"2020022408400831700_B67","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1107\/S0021889809000338","article-title":"DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering","volume":"42","author":"Franke","year":"2009","journal-title":"J. Appl. Crystallogr."},{"key":"2020022408400831700_B68","doi-asserted-by":"crossref","first-page":"11721","DOI":"10.1021\/bi026296y","article-title":"Myoglobin and Cytochrome b5: A Nuclear Magnetic Resonance Study of a Highly Dynamic Protein Complex","volume":"41","author":"Worrall","year":"2002","journal-title":"Biochemistry"},{"key":"2020022408400831700_B69","doi-asserted-by":"crossref","first-page":"200913551","DOI":"10.1073\/pnas.0913551107","article-title":"Lsr2 is a nucleoid-associated protein that targets AT-rich sequences and virulence genes in Mycobacterium tuberculosis","volume":"107","author":"Gordon","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2020022408400831700_B70","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1038\/nsb0897-657","article-title":"The solution structure of an HMG-I (Y)\u2013DNA complex defines a new architectural minor groove binding motif","volume":"4","author":"Huth","year":"1997","journal-title":"Nat. Struct. Mol. Biol."},{"key":"2020022408400831700_B71","doi-asserted-by":"crossref","first-page":"3316","DOI":"10.1093\/nar\/gkr1247","article-title":"Gene silencing H-NS paralogue StpA forms a rigid protein filament along DNA that blocks DNA accessibility","volume":"40","author":"Lim","year":"2011","journal-title":"Nucleic Acids Res."},{"key":"2020022408400831700_B72","doi-asserted-by":"crossref","first-page":"5525","DOI":"10.1093\/nar\/gky265","article-title":"StpA and Hha stimulate pausing by RNA polymerase by promoting DNA-DNA bridging of H-NS filaments","volume":"46","author":"Boudreau","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"2020022408400831700_B73","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1016\/0092-8674(88)90470-9","article-title":"A physiological role for DNA supercoiling in the osmotic regulation of gene expression in S. typhimurium and E. coli","volume":"52","author":"Higgins","year":"1988","journal-title":"Cell"},{"key":"2020022408400831700_B74","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1085\/jgp.46.1.159","article-title":"Cation transport in Escherichia coli: II. Intracellular chloride concentration","volume":"46","author":"Schultz","year":"1962","journal-title":"J. Gen. Physiol."},{"key":"2020022408400831700_B75","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1111\/j.1462-2920.2008.01748.x","article-title":"Ion transport and osmotic adjustment in Escherichia coli in response to ionic and non-ionic osmotica","volume":"11","author":"Shabala","year":"2009","journal-title":"Environ. Microbiol."},{"key":"2020022408400831700_B76","doi-asserted-by":"crossref","first-page":"846","DOI":"10.1007\/BF01985672","article-title":"High magnesium content of Escherichia coli B","volume":"37","author":"Moncany","year":"1981","journal-title":"Experientia"}],"container-title":["Nucleic Acids Research"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/academic.oup.com\/nar\/article-pdf\/48\/4\/2156\/32615410\/gkz1226.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"http:\/\/academic.oup.com\/nar\/article-pdf\/48\/4\/2156\/32615410\/gkz1226.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2020,2,24]],"date-time":"2020-02-24T08:42:38Z","timestamp":1582533758000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/nar\/article\/48\/4\/2156\/5700550"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,1,11]]},"references-count":76,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2020,1,11]]},"published-print":{"date-parts":[[2020,2,28]]}},"URL":"https:\/\/doi.org\/10.1093\/nar\/gkz1226","relation":{"has-review":[{"id-type":"doi","id":"10.3410\/f.737196844.793569585","asserted-by":"object"}],"has-preprint":[{"id-type":"doi","id":"10.1101\/757732","asserted-by":"object"}]},"ISSN":["0305-1048","1362-4962"],"issn-type":[{"value":"0305-1048","type":"print"},{"value":"1362-4962","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2020,2,28]]},"published":{"date-parts":[[2020,1,11]]}}}