A putative lipoprotein of Sphingomonas sp. strain A1 binds alginate rather than a lipid moiety.
Gram-negative Sphingomonas sp. strain A1 accumulates alginate in the cell surface pit and directly incorporates the polysaccharide into its cytoplasm through a 'superchannel'. A cell surface protein Algp7 (27 kDa) is inducibly expressed in the presence of alginate. Although the protein Algp7 was initially classified as a lipoprotein based on its primary structure, Algp7 purified from strain A1 cells did not possess a lipid moiety. Algp7 bound alginate efficiently at a neutral pH with a K(d) of 3.6 x 10(-8) M, suggesting that the cell surface protein contributed to accumulation of alginate in the pit.
He
Jinshan
J
Laboratory of Basic and Applied Molecular Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Kyoto, Japan.
Ochiai
Akihito
A
Fukuda
Yasuki
Y
Hashimoto
Wataru
W
Murata
Kousaku
K
D000464:Alginates / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D020723:Glucuronic Acid / Q000378:metabolism; D006603:Hexuronic Acids / Q000378:metabolism; D008074:Lipoproteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D020578:Sphingomonas / Q000235:genetics / Q000378:metabolism*; D020349:Surface Plasmon Resonance
D000464:Alginates; D006603:Hexuronic Acids; D008074:Lipoproteins; D008565:Membrane Proteins; D020723:Glucuronic Acid