{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,19]],"date-time":"2026-03-19T09:27:06Z","timestamp":1773912426246,"version":"3.50.1"},"reference-count":39,"publisher":"Proceedings of the National Academy of Sciences","issue":"39","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2008,9,30]]},"abstract":"<jats:p>\n            At an early stage during\n            <jats:italic>Bacillus subtilis<\/jats:italic>\n            endospore development the bacterium divides asymmetrically to produce two daughter cells. The smaller cell (forespore) differentiates into the endospore, while the larger cell (mother cell) becomes a terminally differentiated cell that nurtures the developing forespore. During development the mother cell engulfs the forespore to produce a protoplast, surrounded by two bilayer membranes, which separate it from the cytoplasm of the mother cell. The activation of \u03c3\n            <jats:sup>G<\/jats:sup>\n            , which drives late gene expression in the forespore, follows forespore engulfment and requires expression of the\n            <jats:italic>spoIIIA<\/jats:italic>\n            locus in the mother cell. One of the\n            <jats:italic>spoIIIA<\/jats:italic>\n            -encoded proteins SpoIIIAH is targeted specifically to the membrane surrounding the forespore, through an interaction of its C-terminal extracellular domain with the C-terminal extracellular domain of the forespore membrane protein SpoIIQ. We identified a homologous relationship between the C-terminal domain of SpoIIIAH and the YscJ\/FliF protein family, members of which form multimeric rings involved in type III secretion systems and flagella. If SpoIIIAH forms a similar ring structure, it may also form a channel between the mother cell and forespore membranes. To test this hypothesis we developed a compartmentalized biotinylation assay, which we used to show that the C-terminal extracellular domain of SpoIIIAH is accessible to enzymatic modification from the forespore cytoplasm. These and other results lead us to suggest that SpoIIIAH forms part of a channel between the forespore and mother cell that is required for the activation of \u03c3\n            <jats:sup>G<\/jats:sup>\n            .\n          <\/jats:p>","DOI":"10.1073\/pnas.0806301105","type":"journal-article","created":{"date-parts":[[2008,9,24]],"date-time":"2008-09-24T01:27:34Z","timestamp":1222219654000},"page":"15100-15105","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":93,"title":["A channel connecting the mother cell and forespore during bacterial endospore formation"],"prefix":"10.1073","volume":"105","author":[{"given":"Jeffrey","family":"Meisner","sequence":"first","affiliation":[{"name":"*Department of Microbiology and Immunology, Emory University School of Medicine, Atlanta, GA 30322; and"}]},{"given":"Xin","family":"Wang","sequence":"additional","affiliation":[{"name":"*Department of Microbiology and Immunology, Emory University School of Medicine, Atlanta, GA 30322; and"}]},{"given":"Monica","family":"Serrano","sequence":"additional","affiliation":[{"name":"Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica, Universidade Nova de Lisboa, Avenida da Rep\u00fablica, Apartado 127, 2781-901 Oeiras Codex, Portugal"}]},{"given":"Adriano O.","family":"Henriques","sequence":"additional","affiliation":[{"name":"Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica, Universidade Nova de Lisboa, Avenida da Rep\u00fablica, Apartado 127, 2781-901 Oeiras Codex, Portugal"}]},{"suffix":"Jr","given":"Charles P.","family":"Moran","sequence":"additional","affiliation":[{"name":"*Department of Microbiology and Immunology, Emory University School of Medicine, Atlanta, GA 30322; and"}]}],"member":"341","published-online":{"date-parts":[[2008,9,30]]},"reference":[{"key":"e_1_3_3_1_2","doi-asserted-by":"publisher","DOI":"10.1128\/br.40.4.908-962.1976"},{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.mib.2004.10.001"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1128\/MMBR.68.2.234-262.2004"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1101\/gad.1252704"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2005.04501.x"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/gki408"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1093\/bioinformatics\/bti125"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.284.5418.1322"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature03554"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.191378598"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1286-4579(01)01512-X"},{"key":"e_1_3_3_12_2","doi-asserted-by":"publisher","DOI":"10.1006\/jsbi.1998.4048"},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2008.06289.x"},{"key":"e_1_3_3_14_2","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(89)90421-2"},{"key":"e_1_3_3_15_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.090087297"},{"key":"e_1_3_3_16_2","doi-asserted-by":"publisher","DOI":"10.1110\/ps.8.4.921"},{"key":"e_1_3_3_17_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.88.22.9934"},{"key":"e_1_3_3_18_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.1997.3181680.x"},{"key":"e_1_3_3_19_2","doi-asserted-by":"publisher","DOI":"10.1101\/gad.3.11.1735"},{"key":"e_1_3_3_20_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.173.9.2977-2984.1991"},{"key":"e_1_3_3_21_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.177.23.7003-7006.1995"},{"key":"e_1_3_3_22_2","doi-asserted-by":"publisher","DOI":"10.1101\/gad.1039902"},{"key":"e_1_3_3_23_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1534-5807(01)00094-6"},{"key":"e_1_3_3_24_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)93825-1"},{"key":"e_1_3_3_25_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.89.19.9257"},{"key":"e_1_3_3_26_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2005.04811.x"},{"key":"e_1_3_3_27_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.1999.01255.x"},{"key":"e_1_3_3_28_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.96.25.14553"},{"key":"e_1_3_3_29_2","doi-asserted-by":"publisher","DOI":"10.1128\/mr.57.1.50-108.1993"},{"key":"e_1_3_3_30_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M606056200"},{"key":"e_1_3_3_31_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.2003.03651.x"},{"key":"e_1_3_3_32_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.molcel.2006.05.019"},{"key":"e_1_3_3_33_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.micro.57.030502.090832"},{"key":"e_1_3_3_34_2","first-page":"811","article-title":"The type III secretion injectisome","volume":"4","author":"Cornelis GR","year":"2006","unstructured":"GR Cornelis, The type III secretion injectisome. 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