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In this study, we demonstrate that the DNA binding property of MtHU is regulated by posttranslational modifications akin to eukaryotic histones. MtHU purified from <jats:italic>M. tuberculosis<\/jats:italic> cells is found to be acetylated on multiple lysine residues unlike the <jats:italic>E. coli<\/jats:italic> expressed recombinant protein. Using coimmunoprecipitation assay, we identified Eis as one of the acetyl transferases that interacts with MtHU and modifies it. Although Eis is known to acetylate aminoglycosides, the kinetics of acetylation showed that its protein acetylation activity on MtHU is robust. <jats:italic>In vitro<\/jats:italic> Eis modified MtHU at various lysine residues, primarily those located at the carboxyl terminal domain. Acetylation of MtHU caused reduced DNA interaction and alteration in DNA compaction ability of the NAP. Over\u2010expression of the Eis leads to hyperacetylation of HU and decompaction of genome. These results provide first insights into the modulation of the nucleoid structure by lysine acetylation in bacteria.<\/jats:p>","DOI":"10.1111\/mmi.13339","type":"journal-article","created":{"date-parts":[[2016,1,28]],"date-time":"2016-01-28T09:03:17Z","timestamp":1453971797000},"page":"577-588","source":"Crossref","is-referenced-by-count":121,"title":["Lysine acetylation of the <i>Mycobacterium tuberculosis<\/i> HU protein modulates its DNA binding and genome organization"],"prefix":"10.1111","volume":"100","author":[{"given":"Soumitra","family":"Ghosh","sequence":"first","affiliation":[{"name":"Department of Microbiology and Cell biology Indian Institute of Science Bangalore Karnataka 560012 India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bhavna","family":"Padmanabhan","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Cell biology Indian Institute of Science Bangalore Karnataka 560012 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