{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T08:08:18Z","timestamp":1791274098228,"version":"4.1.0"},"reference-count":30,"publisher":"American Society for Microbiology","issue":"22","license":[{"start":{"date-parts":[[2001,11,15]],"date-time":"2001-11-15T00:00:00Z","timestamp":1005782400000},"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":[[2001,11,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The polysaccharide chains of enterobacterial common antigen (ECA) are comprised of the trisaccharide repeat unit Fuc4NAc-ManNAcA-GlcNAc, where Fuc4NAc is 4-acetamido-4,6-dideoxy\n            <jats:sc>-d-<\/jats:sc>\n            galactose, ManNAcA is\n            <jats:italic>N<\/jats:italic>\n            -acetyl\n            <jats:sc>-d-<\/jats:sc>\n            mannosaminuronic acid, and GlcNAc is\n            <jats:italic>N<\/jats:italic>\n            -acetyl\n            <jats:sc>-d-<\/jats:sc>\n            glucosamine. Individual trisaccharide repeat units are assembled as undecaprenyl-linked intermediates in a sequence of reactions that culminate in the transfer of Fuc4NAc from TDP-Fuc4NAc to ManNAcA-GlcNAc-pyrophosphorylundecaprenol (lipid II) to yield Fuc4NAc-ManNAcA-GlcNAc-pyrophosphorylundecaprenol (lipid III), the donor of trisaccharide repeat units for ECA polysaccharide chain elongation. Most of the genes known to be involved in ECA assembly are located in the\n            <jats:italic>wec<\/jats:italic>\n            gene cluster located at ca. 85.4 min on the\n            <jats:italic>Escherichia coli<\/jats:italic>\n            chromosome. The available data suggest that the structural gene for the TDP-Fuc4NAc:lipid II Fuc4NAc transferase also resides in the\n            <jats:italic>wec<\/jats:italic>\n            gene cluster; however, the location of this gene has not been unequivocally defined. Previous characterization of the nucleotide sequence of the\n            <jats:italic>wec<\/jats:italic>\n            gene cluster in the region between\n            <jats:italic>o416<\/jats:italic>\n            and\n            <jats:italic>wecG<\/jats:italic>\n            revealed that it contained three open reading frames:\n            <jats:italic>o74<\/jats:italic>\n            ,\n            <jats:italic>o204<\/jats:italic>\n            , and\n            <jats:italic>o450<\/jats:italic>\n            . In contrast, the results of experiments described in the current investigation revealed that it contains only two open reading frames,\n            <jats:italic>o359<\/jats:italic>\n            and\n            <jats:italic>o450<\/jats:italic>\n            . Mutants of\n            <jats:italic>E. coli<\/jats:italic>\n            possessing null mutations in\n            <jats:italic>o359<\/jats:italic>\n            were unable to synthesize ECA, and they accumulated lipid II. In addition, the in vitro incorporation of [\n            <jats:sup>3<\/jats:sup>\n            H]FucNAc from TDP-[\n            <jats:sup>3<\/jats:sup>\n            H]Fuc4NAc into lipid II was not observed in reaction mixtures using cell extracts obtained from these mutants as a source of enzyme. The ECA-negative phenotype of these mutants was complemented by plasmid constructs containing the wild-type\n            <jats:italic>o359<\/jats:italic>\n            allele, and Fuc4NAc transferase activity was demonstrated by using cell extracts obtained from the complemented mutants. Furthermore, partially purified\n            <jats:italic>o359<\/jats:italic>\n            gene product, expressed as recombinant C-terminal His-tagged protein, was able to catalyze the in vitro transfer of [\n            <jats:sup>3<\/jats:sup>\n            H]Fuc4NAc from TDP-[\n            <jats:sup>3<\/jats:sup>\n            H]Fuc4NAc to lipid II. Our data support the conclusion that\n            <jats:italic>o359<\/jats:italic>\n            of the\n            <jats:italic>wec<\/jats:italic>\n            gene cluster of\n            <jats:italic>E. coli<\/jats:italic>\n            is the structural gene for the TDP-Fuc4NAc:lipid II Fuc4NAc transferase involved in the synthesis ECA trisaccharide repeat units.\n          <\/jats:p>","DOI":"10.1128\/jb.183.22.6509-6516.2001","type":"journal-article","created":{"date-parts":[[2002,7,27]],"date-time":"2002-07-27T09:58:18Z","timestamp":1027763898000},"page":"6509-6516","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":26,"title":["Identification of the Structural Gene for the TDP-Fuc4NAc:Lipid II Fuc4NAc Transferase Involved in Synthesis of Enterobacterial Common Antigen in\n            <i>Escherichia coli<\/i>\n            K-12"],"prefix":"10.1128","volume":"183","author":[{"given":"Arifur","family":"Rahman","sequence":"first","affiliation":[{"name":"<!--label omitted: 1-->Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, Bethesda, Maryland 20814-4799"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kathleen","family":"Barr","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, Bethesda, Maryland 20814-4799"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paul D.","family":"Rick","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, Bethesda, Maryland 20814-4799"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.147.2.602-611.1981"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.181.20.6564-6568.1999"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.171.3.1326-1332.1989"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)48216-6"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.277.5331.1453"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1128\/jcm.24.3.330-332.1986"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.144.1.425-427.1980"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.180.22.5875-5884.1998"},{"key":"e_1_3_2_10_2","doi-asserted-by":"crossref","first-page":"771","DOI":"10.1126\/science.1379743","article-title":"Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes","volume":"257","author":"Daniels D. 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