Function-unknown glycoside hydrolase family 31 proteins, mRNAs of which were expressed in rice ripening and germinating stages, are α-glucosidase and α-xylosidase

被引：18

作者：

Nakai, Hiroyuki ^{[1
]}

Tanizawa, Shigeki ^{[1
]}

Ito, Tatsuya ^{[1
]}

Kamiya, Koutarou ^{[1
]}

Kim, Young-Min ^{[1
]}

Yamamoto, Takeshi ^{[1
]}

Matsubara, Kazuki ^{[1
]}

Sakai, Makoto ^{[2
]}

Sato, Hiroyuki ^{[3
]}

Imbe, Tokio ^{[4
]}

Okuyama, Masayuki ^{[1
]}

Mori, Haruhide ^{[1
]}

Sano, Yoshio ^{[1
]}

Chiba, Seiya ^{[1
]}

Kimura, Atsuo ^{[1
]}

机构：

[1] Hokkaido Univ, Grad Sch Agr, Sapporo, Hokkaido 0608589, Japan

[2] Natl Agr Res Ctr, Chikugo 8330041, Japan

[3] Natl Inst Crop Sci, Tsukuba, Ibaraki 3058518, Japan

[4] Japan Int Ctr Agr Sci, Ishigaki, Okinawa 9070002, Japan

来源：

JOURNAL OF BIOCHEMISTRY | 2007年 / 142卷 / 04期

关键词：

alpha-glucosidase; alpha-xylosidase; glycoside hydrolase family 31; Pichia pastoris; starch granule-binding;

D O I：

10.1093/jb/mvm174

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

In rice (Oryza sativa L., var Nipponbare) seeds, there were three mRNAs encoding for function-unknown hydrolase family 31 homologous proteins (ONGX-H1, ONGX-H3 and ONGX-H4): ONGX-H1 mRNA was expressed in ripening stage and mRNAs of ONGX-H3 and ONGX-H4 were found in both the ripening and germinating stages [Nakai et al., (2007) Biochimie 89, 49-62]. This article describes that the recombinant proteins of ONGX-H1 (rONGXG-H1), ONGX-H3 (rONGXG-H3) and ONG-H4 (rONGXG-H4) were overproduced in Pichia pastoris as fusion protein with the alpha-factor signal peptide of Saccharomyces cerevisiae. Purified rONGXG-H1 and rONGXG-H3 efficiently hydrolysed malto-oligosaccharides, kojibiose, nigerose and soluble starch, indicating that ONGX-H1 and ONGX-H3 are alpha-glucosidases. Their substrate specificities were similar to that of ONG2, a main alpha-glucosidase in the dry and germinating seeds. The rONGXG-H1 and rONGX-H3 demonstrated the lower ability to adsorb to and degradation of starch granules than ONG2 did, suggesting that three a-glucosidases, different in action to starch granules, were expressed in ripening stage. Additionally, purified rONGXG-H4 showed the high activity towards alpha-xylosides, in particular, xyloglucan oligosaccharides. The enzyme hardly hydrolysed alpha-glucosidic linkage, so that ONGX-H4 was an alpha-xylosidase. alpha-Xylosidase encoded in rice genome was found for the first time.

引用

页码：491 / 500

页数：10

共 42 条

[1]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[2] STRUCTURAL MODELS OF PRIMARY-CELL WALLS IN FLOWERING PLANTS - CONSISTENCY OF MOLECULAR-STRUCTURE WITH THE PHYSICAL-PROPERTIES OF THE WALLS DURING GROWTH [J].

CARPITA, NC ;

GIBEAUT, DM .

PLANT JOURNAL, 1993, 3 (01) :1-30

[3] Mechanical effects of plant cell wall enzymes on cellulose/xyloglucan composites [J].

Chanliaud, E ;

De Silva, J ;

Strongitharm, B ;

Jeronimidis, G ;

Gidley, MJ .

PLANT JOURNAL, 2004, 38 (01) :27-37

[4] RECENT ADVANCES IN THE EXPRESSION OF FOREIGN GENES IN PICHIA-PASTORIS [J].

CREGG, JM ;

VEDVICK, TS ;

RASCHKE, WC .

BIO-TECHNOLOGY, 1993, 11 (08) :905-910

[5] A xyloglucan oligosaccharide-active, transglycosylating β-D-glucosidase from the cotyledons of nasturtium (Tropaeolum majus L) seedlings -: purification, properties and characterization of a cDNA clone [J].

Crombie, HJ ;

Chengappa, S ;

Hellyer, A ;

Reid, JSG .

PLANT JOURNAL, 1998, 15 (01) :27-38

[6] Molecular characterisation of a xyloglucan oligosaccharide-acting α-D-xylosidase from nasturtium (Tropaeolum majus L.) cotyledons that resembles plant 'apoplastic' α-D-glucosidases [J].

Crombie, HJ ;

Chengappa, S ;

Jarman, C ;

Sidebottom, C ;

Reid, JSG .

PLANTA, 2002, 214 (03) :406-413

[7] MODEL FOR STARCH BREAKDOWN IN HIGHER-PLANTS [J].

DUNN, G .

PHYTOCHEMISTRY, 1974, 13 (08) :1341-1346

[8] XYLOGLUCAN (AMYLOID) MOBILIZATION IN THE COTYLEDONS OF TROPAEOLUM-MAJUS L SEEDS FOLLOWING GERMINATION [J].

EDWARDS, M ;

DEA, ICM ;

BULPIN, PV ;

REID, JSG .

PLANTA, 1985, 163 (01) :133-140

[9] ISOLATION OF ALCOHOL OXIDASE AND 2 OTHER METHANOL REGULATABLE GENES FROM THE YEAST PICHIA-PASTORIS [J].

ELLIS, SB ;

BRUST, PF ;

KOUTZ, PJ ;

WATERS, AF ;

HARPOLD, MM ;

GINGERAS, TR .

MOLECULAR AND CELLULAR BIOLOGY, 1985, 5 (05) :1111-1121

[10] Purification, enzymatic characterization, and nucleotide sequence of a high-isoelectric-point α-glucosidase from barley malt [J].

Frandsen, TP ;

Lok, F ;

Mirgorodskaya, E ;

Roepstorff, P ;

Svensson, B .

PLANT PHYSIOLOGY, 2000, 123 (01) :275-286

← 1 2 3 4 5 →