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Through a bacterial two-hybrid library screen, we identified the\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">E. coli<\/jats:named-content>\n            \u03b2-lactam resistance protein Blr, a short membrane polypeptide of 41 residues, as an interacting partner of the essential cell division protein FtsL. In addition to FtsL, Blr was found to associate with several other divisomal proteins, including FtsI, FtsK, FtsN, FtsQ, FtsW, and YmgF. Using fluorescently tagged Blr, we showed that this peptide localizes to the division septum and that its colocalization requires the presence of the late division protein FtsN. Although Blr is not essential, previous studies have shown that the inactivation of the\n            <jats:italic>blr<\/jats:italic>\n            gene increased the sensitivity of bacteria to \u03b2-lactam antibiotics or their resistance to cell envelope stress. Here, we found that Blr, when overproduced, restores the viability of\n            <jats:italic>E. coli ftsQ1<\/jats:italic>\n            (Ts) cells, carrying a thermosensitive allele of the\n            <jats:italic>ftsQ<\/jats:italic>\n            gene, during growth under low-osmotic-strength conditions (e.g., in synthetic media or in Luria-Bertani broth without NaCl). In contrast, the inactivation of\n            <jats:italic>blr<\/jats:italic>\n            increases the osmosensitivity of\n            <jats:italic>ftsQ1<\/jats:italic>\n            (Ts) cells, and\n            <jats:italic>blr ftsQ1<\/jats:italic>\n            double mutants exhibit filamentous growth in LB broth even at a moderate salt concentration (0.5% NaCl) compared to parental\n            <jats:italic>ftsQ1<\/jats:italic>\n            (Ts) cells. Altogether, our results suggest that the small membrane polypeptide Blr is a novel component of the\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">E. coli<\/jats:named-content>\n            cell division apparatus involved in the stabilization of the divisome under certain stress conditions.\n          <\/jats:p>","DOI":"10.1128\/jb.00774-12","type":"journal-article","created":{"date-parts":[[2012,8,12]],"date-time":"2012-08-12T02:10:22Z","timestamp":1344737422000},"page":"5576-5588","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":45,"title":["The \u03b2-Lactam Resistance Protein Blr, a Small Membrane Polypeptide, Is a Component of the Escherichia coli Cell Division Machinery"],"prefix":"10.1128","volume":"194","author":[{"given":"Gouzel","family":"Karimova","sequence":"first","affiliation":[{"name":"Institut Pasteur, CNRS UMR 3528, Unit\u00e9 de Biochimie des Interactions Macromol\u00e9culaires, D\u00e9partement de Biologie Structurale et Chimie, Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marilyne","family":"Davi","sequence":"additional","affiliation":[{"name":"Institut Pasteur, CNRS UMR 3528, Unit\u00e9 de Biochimie des Interactions Macromol\u00e9culaires, D\u00e9partement de Biologie Structurale et Chimie, Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel","family":"Ladant","sequence":"additional","affiliation":[{"name":"Institut Pasteur, CNRS UMR 3528, Unit\u00e9 de Biochimie des Interactions Macromol\u00e9culaires, D\u00e9partement de Biologie Structurale et Chimie, Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","first-page":"36","article-title":"Image processing with ImageJ","volume":"11","author":"Abr\u00e0moff MD","year":"2004","unstructured":"Abr\u00e0moffMDMagalh\u00e3esPJRamSJ. 2004. 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