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Recent\nwork in our laboratory has shown that Wzx proteins involved in\nO-antigen lipopolysaccharide (LPS) assembly have relaxed specificity\nfor the carbohydrate structure of the O-antigen subunit. Furthermore,\nthe proximal sugar bound to the isoprenoid lipid carrier,\nundecaprenyl-phosphate (Und-P), is the minimal structure required for\ntranslocation. In\n            <jats:italic>Escherichia coli<\/jats:italic>\n            K-12,\n            <jats:italic>N<\/jats:italic>\n            -acetylglucosamine (GlcNAc) is the proximal sugar of\nthe O16 and enterobacterial common antigen (ECA) subunits. Both O16 and\nECA systems have their respective translocases, Wzx\n            <jats:sub>O16<\/jats:sub>\n            and\nWzx\n            <jats:sub>E<\/jats:sub>\n            , and also corresponding polymerases (Wzy\n            <jats:sub>O16<\/jats:sub>\n            and Wzy\n            <jats:sub>E<\/jats:sub>\n            ) and O-antigen chain-length regulators\n(Wzz\n            <jats:sub>O16<\/jats:sub>\n            and Wzz\n            <jats:sub>E<\/jats:sub>\n            ), respectively. In\nthis study, we show that the\n            <jats:italic>E. coli wzx<\/jats:italic>\n            <jats:sub>E<\/jats:sub>\n            gene can\nfully complement a\n            <jats:italic>wzx<\/jats:italic>\n            <jats:sub>O16<\/jats:sub>\n            translocase deletion\nmutant only if the majority of the ECA gene cluster is deleted. In\naddition, we demonstrate that introduction of plasmids expressing\neither the Wzy\n            <jats:sub>E<\/jats:sub>\n            polymerase or the Wzz\n            <jats:sub>E<\/jats:sub>\n            chain-length regulator proteins drastically reduces the O16\nLPS-complementing activity of Wzx\n            <jats:sub>E<\/jats:sub>\n            . We also show that this\nproperty is not unique to Wzx\n            <jats:sub>E<\/jats:sub>\n            , since Wzx\n            <jats:sub>O16<\/jats:sub>\n            and\nWzx\n            <jats:sub>O7<\/jats:sub>\n            can cross-complement translocase defects in the O16\nand O7 antigen clusters only in the absence of their corresponding Wzz\nand Wzy proteins. These genetic data are consistent with the notion\nthat the translocation of O-antigen and ECA subunits across the plasma\nmembrane and the subsequent assembly of periplasmic O-antigen and ECA\nUnd-PP-linked polymers depend on interactions among Wzx, Wzz, and Wzy,\nwhich presumably form a multiprotein\ncomplex.\n          <\/jats:p>","DOI":"10.1128\/jb.00461-06","type":"journal-article","created":{"date-parts":[[2006,6,30]],"date-time":"2006-06-30T23:17:58Z","timestamp":1151709478000},"page":"5124-5135","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":87,"title":["Interplay of the Wzx Translocase and the Corresponding Polymerase and Chain LengthRegulator Proteins in the Translocation and Periplasmic Assembly of Lipopolysaccharide O Antigen"],"prefix":"10.1128","volume":"188","author":[{"given":"Cristina L.","family":"Marolda","sequence":"first","affiliation":[{"name":"Infectious Diseases Research Group, Siebens-Drake Medical Research Institute, Department of Microbiology and Immunology and Department of Medicine, University of Western Ontario, London, Ontario, Canada, N6A 5C1"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laura D.","family":"Tatar","sequence":"additional","affiliation":[{"name":"Infectious Diseases Research Group, Siebens-Drake Medical Research Institute, Department of Microbiology and Immunology and Department of Medicine, University of Western Ontario, London, Ontario, Canada, N6A 5C1"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cristina","family":"Alaimo","sequence":"additional","affiliation":[{"name":"Institute of Microbiology, Department of Biology, Swiss Federal Institute of Technology, ETH-Ho\u0308nggeberg, CH-8093 Zurich, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Markus","family":"Aebi","sequence":"additional","affiliation":[{"name":"Institute of Microbiology, Department of Biology, Swiss Federal Institute of Technology, ETH-Ho\u0308nggeberg, CH-8093 Zurich, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Miguel A.","family":"Valvano","sequence":"additional","affiliation":[{"name":"Infectious Diseases Research Group, Siebens-Drake Medical Research Institute, Department of Microbiology and Immunology and Department of Medicine, University of Western Ontario, London, Ontario, Canada, N6A 5C1"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1038\/sj.emboj.7601024","volume":"25","year":"2006","unstructured":"Alaimo, C., I. 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