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Originally published In Press as doi:10.1074/jbc.M206808200 on September 15, 2002

J. Biol. Chem., Vol. 277, Issue 48, 45719-45728, November 29, 2002
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Characterization of the Second Type of Human beta -Galactoside alpha 2,6-Sialyltransferase (ST6Gal II), Which Sialylates Galbeta 1,4GlcNAc Structures on Oligosaccharides Preferentially
GENOMIC ANALYSIS OF HUMAN SIALYLTRANSFERASE GENES*

Shou TakashimaDagger §, Shuichi Tsuji, and Masafumi TsujimotoDagger ||

From the Dagger  Laboratory of Cellular Biochemistry, RIKEN (The Institute of Physical and Chemical Research), 2-1 Hirosawa, Wako, Saitama 351-0198 and  Department of Chemistry, Faculty of Science, Ochanomizu University, Otsuka, Bunkyo-ku, Tokyo 112-8610, Japan

A novel member of the human beta -galactoside alpha 2,6-sialyltransferase (ST6Gal) family, designated ST6Gal II, was identified by BLAST analysis of expressed sequence tags and genomic sequences. The sequence of ST6Gal II encoded a protein of 529 amino acids, and it showed 48.9% amino acid sequence identity with human ST6Gal I. Recombinant ST6Gal II exhibited alpha 2,6-sialyltransferase activity toward oligosaccharides that have the Galbeta 1,4GlcNAc sequence at the nonreducing end of their carbohydrate groups, but it exhibited relatively low and no activities toward some glycoproteins and glycolipids, respectively. It is concluded that ST6Gal II is an oligosaccharide-specific enzyme compared with ST6Gal I, which exhibits broad substrate specificities, and is mainly involved in the synthesis of sialyloligosaccharides. The expression of the ST6Gal II gene was significantly detected by reverse transcription PCR in small intestine, colon, and fetal brain, whereas the ST6Gal I gene was ubiquitously expressed, and its expression levels were much higher than those of the ST6Gal II gene. The ST6Gal I gene was also expressed in all tumors examined, but no expression was observed for the ST6Gal II gene in these tumors. The ST6Gal II gene is located on chromosome 2 (2q11.2-q12.1), and it spans over 85 kb of human genomic DNA consisting of at least eight exons and shares a similar genomic structure with the ST6Gal I gene. In this paper, we have shown that ST6Gal I, which has been known as the sole member of the ST6Gal family, also has the counterpart enzyme (ST6Gal II) like other sialyltransferases.


* This work was supported in part by a grant for the "Multibioprobe Research Program" from RIKEN (The Institute of Physical and Chemical Research).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the DDBJ/GenBankTM/EBI Data Bank with accession number(s) AB059555.

§ Special postdoctoral researcher from RIKEN (The Institute of Physical and Chemical Research).

|| To whom correspondence should be addressed. Tel.: 81-48-467-9370; Fax: 81-48-462-4670; E-mail: tsujimot@postman.riken.go.jp.


Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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