1520
Y.O. Ahn et al. / Phytochemistry 68 (2007) 1510–1520
Cicek, M., Esen, A., 1999. Expression of soluble catalytically active plant
(monocot) b-glucosidases in E. coli. Biotechnol. Bioeng. 63, 392–400.
Coutinho, P.M., Henrissat, B., 1999. Carbohydrate-active enzymes: an
integrated database approach. In: Gilbert, H.J., Davies, G., Henrissat,
B., Svensson, B. (Eds.), . In: Recent Advances in Carbohydrate
Bioengineering. The Royal Society of Chemistry, Cambridge, pp. 3–12.
Pressey, R., 1983. b-Galactosidases in ripening tomatoes. Plant Physiol.
71, 132–135.
Prinz, W.A., Aslund, F., Holmgren, A., Beckwith, J., 1997. The role of the
thioredoxin and glutaredoxin pathways in reducing protein disulfide
bonds in the Escherichia coli cytoplasm. J. Biol. Chem. 272, 15661–
15667.
ˆ
de Alicantara, P.H.N., Dietrich, S.M.B., Buckeridge, M.S., 1999. Xylo-
Ragothama, K.G., Lawton, K.A., Goldsborough, P.B., Woodson, W.R.,
1991. Characterization of an ethylene-regulated flower senescence-
related gene from carnation. Plant Mol. Biol. 17, 61–71.
Ross, G.S., Wegrzyn, T., MacRae, E.A., Redgwell, R.J., 1994. Apple b-
galactosidase activity against cell wall polysaccharides and character-
ization of a related cDNA clone. Plant Physiol. 106, 521–528.
Saitou, N., Nei, M., 1987. The neighbor-joining method: a new method for
reconstructing phylogenetic trees. Mol. Biol. Evol. 4, 406–425.
Schmid, M., Davison, T.S., Henz, S.R., Pape, U.J., Demar, M., Vingron,
M., Scho¨lkopf, B., Weigel, D., Lohmann, J., 2005. A gene expression
map of Arabidopsis development. Nature Genet. 37, 501–506.
Schmittgen, T.D., Zakrajsek, B.A., Mills, A.G., Gorn, V., Singer, M.J.,
Reed, M.W., 2000. Quantitative reverse transcription-polymerase
chain reaction to study mRNA decay: comparison of endpoint and
real-time methods. Anal. Biochem. 285, 194–204.
glucan mobilization and purification of a (XLLG/XLXG) specific b-
galactosidase from cotyledons of Copaifera langsdorfii. Plant Physiol.
Biochem. 37, 653–663.
Dey, P.M., del Campillo, E., 1984. Biochemistry of the multiple forms of
glycosidases in plants. In: Meister, A. (Ed.), . In: Adv. Enzymol. Relat.
Areas Mol. Biol., Vol. 56. Wiley, New York, pp. 141–249.
Dopico, B., Nicolas, G., Labrador, E., 1989. Partial purification of cell
wall b-galactosidases from Cicer arietinum epicotyls. Physiol. Plant 75,
458–464.
Edwards, M., Bowman, Y.J., Dea, I.C., Reid, J.S., 1988. A b-D-
galactosidase from nasturtium (Tropaeolum majus L.) cotyledons.
Purification, properties, and demonstration that xyloglucan is the
natural substrate. J. Biol. Chem. 263, 4333–4337.
Gy, I., Kreis, M., Lecharny, A., 2000. The b-galactosidases are encoded by
a multigene family in A. thaliana. GenBank Accessions CAB64773-
64750.
Schultz, J., Copley, R.R., Doerks, T., Ponting, C.P., Bork, P., 2000.
SMART: a web-based tool for the study of genetically mobile
domains. Nucleic Acids Res. 28, 231–234.
Hamer, B.D., Rickwood, D., 1981. Preparation and electrophoresis of
polyacrylamide gels. In: Hames, B.D., Rickwood, D. (Eds.), Gel
Electrophoresis of Proteins: A Practical Approach. IRL Press Ltd.,
London and Washington, DC, pp. 23–42.
Sekimata, M., Ogura, K., Tsumuraya, Y., Hashimoto, Y., 1989. A b-
galactosidase from radish (Raphanus sativus L.) seeds. Plant Physiol.
90, 567–574.
Henrissat, B., 1998. Glycosidase families. Biochem. Soc. Trans. 26, 153–
156.
Sellner, L.N., Turbett, G.R., 1998. Comparison of three RT-PCR
methods. Biotechniques 25, 230–234.
Higgins, D.G., Thompson, J.D., Gibson, T.J., 1996. Using CLUSTAL for
multiple sequence alignments. Methods Enzymol. 266, 382–402.
Ishimaru, M., Smith, D., Gross, K., 2005. Yeast expressed tomato b-
galactosidases 1, 4 and 5 have activity against synthetic and plant
derived cell wall substrates. Hortscience 40, 1092.
Shiu, S.-H., Karlowski, W.M., Pan, R., Tzeng, Y.H., Mayer, K.F., Li, W.-
H., 2004. Comparative analysis of the receptor-like kinase family in
Arabidopsis and rice. Plant Cell 16, 1220–1234.
Shiu, S.-H., Shih, M.-C., Li, W.-H., 2005. Higher retention rate of
transcription factor families in plants than in animals and their
preferential retention among duplicated plant genes. Plant Physiol.
139, 18–26.
King, G.A., Davies, K.M., 1995. Cloning of a harvest-induced b-
galactosidase from tips of harvested asparagus spears. Plant Physiol.
108, 419–420.
Smith, D.L., Starrett, D.A., Gross, K.C., 1998. A gene coding for tomato
fruit b-galactosidase II is expressed during fruit ripening. Plant
Physiol. 117, 417–423.
Kotake, T., Dina, S., Konishi, T., Kaneko, S., Igarashi, K., Samejima, M.,
Watanabe, Y., Kimura, K., Tsumuraya, Y., 2005. Molecular cloning
of a b-galactosidase from radish that specifically hydrolyzes b-(1 ! 3)-
and b-(1 ! 6)-galactosyl residues of arabinogalactan protein. Plant
Physiol. 138, 1563–1576.
Smith, D.L., Abbott, J.A., Gross, K.C., 2002. Down-regulation of tomato
b-galactosidase 4 results in decreased fruit softening. Plant Physiol.
129, 1755–1762.
Kumar, S., Tamura, K., Nei, M., 2004. MEGA3: Integrated software for
molecular evolutionary genetics analysis and sequence alignment.
Briefings Bioinform. 5, 150–163.
Smith, D.L., Gross, K.C., 2000. A family of at least seven b-galactosidase
genes is expressed during tomato fruit development. Plant Physiol. 123,
1173–1183.
Laemmli, U.K., 1970. Cleavage of structural proteins during the assembly
of the head of bacteriophage T4. Nature 277, 680–685.
Lazan, H., Ng, S.Y., Goh, L.Y., Ali, Z.M., 2004. Papaya b-galactosidase/
galactanase isoforms in differential cell wall hydrolysis and fruit
softening during ripening. Plant Physiol. Biochem. 42, 847–853.
Lee, D.H., Kang, S.G., Suh, S.G., Byun, J.K., 2003. Purification and
characterization of a b-galactosidase from peach (Prunus persica).
Mol. Cells 15, 68–74.
Sonnhammer, E.L.L., Eddy, S.R., Birney, E., Bateman, A., Durbin, R.,
1998. Pfam: multiple sequence alignments and HMM-profiles of
protein domains. Nucleic Acids Res. 26, 320–322.
The Arabidopsis Genome Initiative, 2000. Analysis of the genome
sequence of the flowering plant Arabidopsis thaliana. Nature 408,
796–815.
Triantafillidou, D., Georgatsos, J.G., 2001. Barley b-galactosidase:
structure, function, heterogeneity, and gene origin. J. Protein Chem.
20, 551–562.
Li, S.C., Han, J.W., Chen, K.C., Chen, C.S., 2001. Purification and
characterization of isoform of b-galactosidases in mung bean seedlings.
Phytochemistry 57, 349–359.
Willats, W.G., McCartney, L., Mackie, W., Knox, J.P., 2001. Pectin: cell
biology and prospects for functional analysis. Plant Mol. Biol. 47, 9–
27.
McCarter, J.D., Burgoyne, D.L., Miao, S., Zhang, S., Callahan, J.W.,
Withers, S.G., 1997. Identification of Glu-268 as the catalytic
nucleophile of human lysosomal b-galactosidase precursor by mass
spectrometry. J. Biol. Chem. 272, 396–400.
Yoon, J.H., Ajisaka, K., 1996. The synthesis of galactopyranosyl
derivatives with b-galactosidases of different origins. Carbohyd. Res.
292, 153–163.
Page, R.D.M., Charleston, M.A., 1997. From gene to organismal
phylogeny: reconciled trees and the gene tree/species tree problem.
Mol. Phylogen. Evol. 7, 231–240.
Zablackis, E., Huang, J., Muller, B., Darvill, A.G., Albersheim, P., 1995.
¨
Characterization of the cell-wall polysaccharides of Arabidopsis
thaliana leaves. Plant Physiol. 107, 1129–1138.