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A prerequisite for the synthesis of sialylated glycoconjugates is the activated sugar-nucleotide cytidine 5\u2032-monophosphate\n            <jats:italic>N<\/jats:italic>\n            -acetylneuraminic acid (CMP-Neu5Ac), which provides a substrate for Golgi sialyltransferases. Although a mammalian enzymatic activity responsible for the synthesis of CMP-Neu5Ac has been described and the enzyme has been purified to near homogeneity, sequence information is restricted to bacterial CMP-Neu5Ac synthetases. In this paper, we describe the molecular characterization, functional expression, and subcellular localization of murine CMP-Neu5Ac synthetase. Cloning was achieved by complementation of the Chinese hamster ovary\n            <jats:italic>lec32<\/jats:italic>\n            mutation that causes a deficiency in CMP-Neu5Ac synthetase activity. A murine cDNA encoding a protein of 432 amino acids rescued the\n            <jats:italic>lec32<\/jats:italic>\n            mutation and also caused polysialic acid to be expressed in the capsule of the CMP-Neu5Ac synthetase negative\n            <jats:italic>Escherichia coli<\/jats:italic>\n            mutant EV5. Three potential nuclear localization signals were found in the murine synthetase, and immunofluorescence studies confirmed predominantly nuclear localization of an N-terminally Flag-tagged molecule. Four stretches of amino acids that occur in the N-terminal region are highly conserved in bacterial CMP-Neu5Ac synthetases, providing evidence for an ancestral relationship between the sialylation pathways of bacterial and animal cells.\n          <\/jats:p>","DOI":"10.1073\/pnas.95.16.9140","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T14:42:40Z","timestamp":1027694560000},"page":"9140-9145","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":115,"title":["Mammalian cytidine 5\u2032-monophosphate\n            <i>N<\/i>\n            -acetylneuraminic acid synthetase: A nuclear protein with evolutionarily conserved structural motifs"],"prefix":"10.1073","volume":"95","author":[{"given":"Anja-K.","family":"M\u00fcnster","sequence":"first","affiliation":[{"name":"Institut f\u00fcr Medizinische Mikrobiologie, Medizinische Hochschule Hannover, Carl-Neuberg-Strasse 1, D-30625 Hannover, Germany; and Department of Cell Biology, Albert Einstein College of Medicine, New York, NY 10461"}]},{"given":"Matthias","family":"Eckhardt","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Medizinische Mikrobiologie, Medizinische Hochschule Hannover, Carl-Neuberg-Strasse 1, D-30625 Hannover, Germany; 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