TY - JOUR
AU - MINAMI, Yuji
AB - Abstract A new galectin was characterized in the Amethyst deceiver mushroom Laccaria amethystina. The complete amino acid (AA) sequence of the lectin, which exhibited β-galactoside specificity, was deduced from its peptide sequences. The AA sequence of L. amethystina galectin (LAG) showed high homology with those of the same genus, at 75.6% identity to Laccaria bicolor, and 35.5–65.0% to galectins of Agrocybe spp. and Coprinopsis cinerea. The AA sequence of LAG contained all but one conserved residue known to be involved in β-galactoside binding, with His at the position 57 residue replaced by Thr in LAG. Analysis of binding specificity by hemagglutination inhibition assay and enzyme-linked lectin-sorbent assay revealed high specificity of LAG towards O-glycoproteins. galectin, amino acid sequence, carbohydrate binding specificity, Laccaria amethystina Reference 1) Roy M, Dubois MP, Proffit M, Vincenot L, Desmarais E, and Selosse M-A, Mol. Ecol., 17, 2825–2838 (2008). 2) Guillot J, Genaud L, Guegunot J, and Damez M, Biochemistry, 22, 5365–5369 (1983). 3) Barondes SH, Castronovo V, Cooper DNW, Cummings RD, Drickamer K, Feizi T, Gitt MA, Hirabayashi J, Hughes C, Kasai K, Effler LH, Liu F, Lotan R, Mercurio AM, Monsigny M, Pillai S, Poirier F, Raz A, Rigby PWJ, Rini JM, and Wang JL, Cell, 76, 597–598 (1994). 4) Cooper DN, Boulianne PR, Charlton S, Farrell EM, Sucher A, and Lu BC, J. Biol. Chem., 272, 1514–1521 (1997). 5) Yagi F, Hiroyama H, and Kodama S, Glycoconj. J., 18, 745–749 (2001). 6) Yang N, Tong X, Xiang Y, Zhang Y, Liang Y, Sun H, and Wang D, J. Biochem., 138, 145–150 (2005). 7) Wälti MA, Walser PJ, Thore S, Grünler A, Bednar B, Künzle M, and Aebi M, J. Mol. Biol., 379, 146–159 (2008). 8) Mueller GM, Mycologia, 77, 121–129 (1985). 9) Elo J and Estola E, Ann. Med. Exp. Biol. Fenn., 30, 165–167 (1952). 10) Raszeja S, Z. Arztl. Fortbild., 58, 801–803 (1964). 11) Martin F, Aerts A, Ahren D, Brun A, Danchin EGJ, Duchaussoy F, Gibon J, Kohler A, Lindquist E, Pereda V, Salamov A, Shapiro HJ, Wuyts J, Blaudez D, Buee M, Brokstein P, Canbaeck B, Cohen D, Courty PE, Coutinho PM, Delaruelle C, Detter JC, Deveau A, DiFazio S, Duplessis S, Fraissinet-Tachet L, Lucic E, Frey-Klett P, Fourrey C, Feussner I, Gay G, Grimwood J, Hoegger PJ, Jain P, Kilaru S, Labbe J, Lin YC, Legue V, Le Tacon F, Marmeisse R, Melayah D, Montanini B, Muratet M, Nehls U, Niculita-Hirzel H, Oudot-Le Secq MP, Peter M, Quesneville H, Rajashekar B, Reich M, Rouhier N, Schmutz J, Yin T, Chalot M, Henrissat B, Kuees U, Lucas S, van de Peer Y, Podila GK, Polle A, Pukkila PJ, Richardson PM, Rouze P, Sanders IR, Stajich JE, Tunlid A, Tuskan G, and Grigoriev IV, Nature, 452, 88–92 (2008). 12) Duk M, Lisowska E, Wu J, and Wu AM, Anal. Biochem., 221, 266–272 (1994). 13) Lowry OH, Rosebrough NJ, Farr AL, and Randal RJ, J. Biol. Chem., 193, 265–275 (1951). 14) Davis BJ, Ann. NY Acad. Sci., 121, 404–427 (1964). 15) Laemmli UK, Nature, 227, 680–685 (1970). 16) Mahoney WC, Smith PK, and Hermodson MA, Biochemistry, 20, 443–448 (1981). 17) Enfield DL, Ericsson LH, Fujikawa K, Walsh KA, Neurath H, and Titani R, Biochemistry, 19, 659–667 (1980). 18) Schagger H, Anal. Biochem., 166, 368–379 (1987). 19) Matsudaira P, J. Biol. Chem., 262, 10035–10038 (1987). 20) Liu YG and Whittier RF, Genomics, 25, 674–681 (1995). 21) Didier E, Didier P, Fargein N, Guillot J, Croisille Y, and Thiery JP, Int. J. Dev. Biol., 34, 421–431 (1990). 22) Hirabayashi J, Hashidate T, Arata Y, Nishi N, Nakamura T, Hirashima M, Urashima T, Oka T, Futai M, Muller EGW, Yagi F, and Kasai K, Biochim. Biophys. Acta, 1572, 232–254 (2002). 23) Oda Y, Herrmann J, Gitt MA, Turck CW, Burlingame AL, Barondes SH, and Leffler H, J. Biol. Chem., 268, 5929–5939 (1993). 24) Marschal P, Herrmann J, Leffler H, Barondes SH, and Cooper DNW, J. Biol. Chem., 267, 12942–12949 (1992). 25) Hanish F-G, Saur A, Muller WRG, Conrad J, and Uhlenbruck G, Biochim. Biophys. Acta, 801, 388–395 (1984). 26) Walser PJ, Haebel PW, Künzler M, Sargent D, Kües U, Aebi M, and Ban N, Structure, 12, 689–702 (2004). 27) Yagi F, Miyamoto M, Abe T, Minami Y, Tadera K, and Goldstein IJ, Glycoconj. J., 14, 281–288 (1997). 28) Tsuji T and Osawa T, Carbohydr. Res., 151, 391–402 (1986). 29) Karlsson NG, Nordman H, Karlsson H, Carlstedt I, and Hansson GC, Biochem. J., 326, 911–917 (1997). 30) Wu AM, J. Biomed. Sci., 10, 676–688 (2003). 31) Leffler H and Barondes SH, J. Biol. Chem., 261, 10119–10126 (1986). 32) Hirabayashi J, Ubukata T, and Kasai K, J. Biol. Chem., 271, 2497–2502 (1996). 33) Larkin MA, Blackshields G, Brown NP, Chenna R, McGettigan PA, McWilliam H, Valentin F, Wallace IM, Wilm A, Lopez R, Thompson JD, Gibson TJ, and Higgins DG, Bioinformatics, 23, 2947–2948 (2007). 34) Hirabayashi J, Satoh T, and Kasai K, J. Biol Chem., 267, 15485–15490 (1992). 35) Ban M, Yoon HJ, Demirkan E, Utsumi S, Mikami B, and Yagi F, J. Mol. Biol., 351, 695–706 (2005). 36) Lobsanov Y, Gitt MA, Leffler H, Barondes SH, and Rini JM, J. Biol. Chem., 268, 27034–27038 (1993). 37) Boulianne RP, Liu Y, Aebi M, Lu BC, and Kües U, Microbiology, 146, 1841–1853 (2000). PDF This content is only available as a PDF. © Japan Society for Bioscience, Biotechnology, and Agrochemistry 2011 This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model) © Japan Society for Bioscience, Biotechnology, and Agrochemistry 2011
TI - Primary Structure and Specificity of a New Member of Galectin Family from the Amethyst Deceiver Mushroom Laccaria amethystina
JO - Bioscience Biotechnology and Biochemistry
DO - 10.1271/bbb.100542
DA - 2011-01-23
UR - https://www.deepdyve.com/lp/oxford-university-press/primary-structure-and-specificity-of-a-new-member-of-galectin-family-ofb9LCuo8X
SP - 62
EP - 69
VL - 75
IS - 1
DP - DeepDyve
ER -