{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T14:03:32Z","timestamp":1791036212528,"version":"4.1.0"},"reference-count":32,"publisher":"American Society for Microbiology","issue":"1","license":[{"start":{"date-parts":[[2005,1,1]],"date-time":"2005-01-01T00:00:00Z","timestamp":1104537600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2005,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:p>MreB is thought to be a bacterial actin homolog that defines the morphology of rod-shaped bacteria.<jats:italic>Rhodobacter sphaeroides<\/jats:italic>changes shape, from a rod to coccobacillus, and undergoes extensive cytoplasmic membrane invagination when it switches from aerobic to photoheterotrophic growth. The role of MreB in defining<jats:italic>R. sphaeroides<\/jats:italic>shape was therefore investigated. Attempts at deleting or insertionally inactivating<jats:italic>mreB<\/jats:italic>were unsuccessful under all growth conditions. Immunofluorescence microscopy showed MreB localized to mid-cell in elongating cells under both aerobic and photoheterotrophic conditions. Three-dimensional reconstruction showed that MreB formed a ring at mid-cell. MreB remained at mid-cell as septation began but localized to new sites in the daughter cells before the completion of septation. MreB localized to putative septation sites in cephalexin-treated filamentous cells. Genomic single-copy<jats:italic>mreB<\/jats:italic>was replaced with<jats:italic>gfp<\/jats:italic>-<jats:italic>mreB<\/jats:italic>, and green fluorescent protein (GFP)-MreB localized in the same pattern, as seen with immunofluorescence microscopy. Some of the cells expressing GFP-MreB were abnormal, principally displaying an increase in cell width, suggesting that the fusion was not fully functional in all cells. GFP-MreB localized to swellings at mid-cell in cells treated with the penicillin-binding protein 2 inhibitor amdinocillin. These data suggest that MreB is essential in<jats:italic>R. sphaeroides<\/jats:italic>, performing a role at mid-cell in elongating cells, and in early septation, putatively in the cytoplasmic control of the peptidoglycan synthetic complexes.<\/jats:p>","DOI":"10.1128\/jb.187.1.54-64.2005","type":"journal-article","created":{"date-parts":[[2004,12,15]],"date-time":"2004-12-15T17:38:20Z","timestamp":1103132300000},"page":"54-64","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":77,"title":["Localization of MreB in<i>Rhodobacter sphaeroides<\/i>under Conditions Causing Changes in Cell Shape and Membrane Structure"],"prefix":"10.1128","volume":"187","author":[{"given":"Peter M.","family":"Slovak","sequence":"first","affiliation":[{"name":"Department of Biochemistry, University of Oxford, Oxford, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"George H.","family":"Wadhams","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Oxford, Oxford, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Judith P.","family":"Armitage","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Oxford, Oxford, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"crossref","first-page":"1053","DOI":"10.1007\/s004380050034","volume":"263","year":"2000","unstructured":"Burger, A., K. 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