J. Biochem, 1998, Vol. 123, No. 1 94-100
© 1998 Japanese Biochemical Society
research-article |
Cloning and Expression of a Marine Bacterial ß-Galactoside 
2,6-Sialyltransferase Gene from Photobacterium damsela JT0160
Sea Water Science Research Laboratory, Japan Tobacco Inc. 4-13-20 Sakawa, Odawara, Kanagawa 256
1To whom correspondence should be addressed at the present address: Tobacco Science Research Laboratory, Japan Tobacco Inc., 6-2 Umegaoka, Aoba-ku, Yokohama, Kanagawa 227. Phone: +81-45-973-5611, Fax: +81-45-973-6781
Sialyltransferase 0160, a bacterial sialyltransferase which catalyzes the incorporation of NeuAc from CMP-NeuAc into the galactose residue of the carbohydrate chain at position 6, is produced by Photobacterium damsels JT0160. The gene coding for sialyltransferase 0160 (bst) was cloned, sequenced, and expressed in Escherichia coli. The sialyltransferase 0160 gene contains an open reading frame of 2, 028 base pairs encoding a protein of 675 amino acid residues. The deduced amino acid sequence of sialyltransferase 0160 did not contain the sialylmotif and had no significant similarity to mammalian sialyltransferases. Crude extracts of cultured E. coli MV1184 cells carrying an expression plasmid for the sialyltransferase 0160 gene showed sialyltransferase activity, which was identified as ß-galactoside 
2,6-sialyltransferase activity by enzymatic reaction product analysis. In addition, when mutant genes, lacking 3'-coding regions for COOH-terminal portions of the protein, which are thought to form -helix structures, were expressed in E. coli MV1184, solubleform enzymes were obtained. This implies that the COOH-terminal portion of sialyltransferase 0160 is required for membrane binding.
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  S. Almagro-Moreno and E. F. Boyd Sialic Acid Catabolism Confers a Competitive Advantage to Pathogenic Vibrio cholerae in the Mouse Intestine Infect. Immun., September 1, 2009; 77(9): 3807 - 3816. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 H. Tsukamoto, Y. Takakura, T. Mine, and T. Yamamoto Photobacterium sp. JT-ISH-224 Produces Two Sialyltransferases, {alpha}-/{beta}-Galactoside {alpha}2,3-Sialyltransferase and {beta}-Galactoside {alpha}2,6-Sialyltransferase J. Biochem., February 1, 2008; 143(2): 187 - 197. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Y. Kakuta, N. Okino, H. Kajiwara, M. Ichikawa, Y. Takakura, M. Ito, and T. Yamamoto Crystal Structure of Vibrionaceae Photobacterium sp. JT-ISH-224 {alpha}2,6-Sialyltransferase in a Ternary Complex With Donor Product CMP and Acceptor Substrate Lactose: Catalytic Mechanism and Substrate Recognition Glycobiology, January 1, 2008; 18(1): 66 - 73. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T. Yamamoto, Y. Hamada, M. Ichikawa, H. Kajiwara, T. Mine, H. Tsukamoto, and Y. Takakura A {beta}-galactoside {alpha}2,6-sialyltransferase produced by a marine bacterium, Photobacterium leiognathi JT-SHIZ-145, is active at pH 8 Glycobiology, November 1, 2007; 17(11): 1167 - 1174. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. Konno, T. Ogawa, T. Shirai, and K. Muramoto Reconstruction of a Probable Ancestral Form of Conger Eel Galectins Revealed Their Rapid Adaptive Evolution Process for Specific Carbohydrate Recognition Mol. Biol. Evol., November 1, 2007; 24(11): 2504 - 2514. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 H. Tsukamoto, Y. Takakura, and T. Yamamoto Purification, Cloning, and Expression of an {alpha}/beta-Galactoside {alpha}-2,3-Sialyltransferase from a Luminous Marine Bacterium, Photobacterium phosphoreum J. Biol. Chem., October 12, 2007; 282(41): 29794 - 29802. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Y. Takakura, H. Tsukamoto, and T. Yamamoto Molecular Cloning, Expression and Properties of an {alpha}/{beta}-Galactoside {alpha}2,3-Sialyltransferase from Vibrio sp. JT-FAJ-16 J. Biochem., September 1, 2007; 142(3): 403 - 412. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Harduin-Lepers, R. Mollicone, P. Delannoy, and R. Oriol The animal sialyltransferases and sialyltransferase-related genes: a phylogenetic approach Glycobiology, August 1, 2005; 15(8): 805 - 817. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. M. Steenbergen, C. A. Lichtensteiger, R. Caughlan, J. Garfinkle, T. E. Fuller, and E. R. Vimr Sialic Acid Metabolism and Systemic Pasteurellosis Infect. Immun., March 1, 2005; 73(3): 1284 - 1294. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
K. Sujino, R. J. Jackson, N. W. C. Chan, S. Tsuji, and M. M. Palcic A novel viral {alpha}2,3-sialyltransferase (v-ST3Gal I): transfer of sialic acid to fucosylated acceptors Glycobiology, March 1, 2000; 10(3): 313 - 320. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
G.-J. Shen, A. K. Datta, M. Izumi, K. M. Koeller, and C.-H. Wong Expression of alpha 2,8/2,9-Polysialyltransferase from Escherichia coli K92. CHARACTERIZATION OF THE ENZYME AND ITS REACTION PRODUCTS J. Biol. Chem., December 3, 1999; 274(49): 35139 - 35146. [Abstract] [Full Text] [PDF]
|
|