Cloning and Sequencing of a cDNA Encoding <i>α</i>-Glucosidase from Sugar Beet

Matsui, Hirokazu; Iwanami, Shunsuke; Ito, Hiroyuki; Mori, Haruhide; Honma, Mamoru; Chiba, Seiya

doi:10.1271/bbb.61.875

Cited by 21 publications

(9 citation statements)

References 4 publications

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“…The deduced amino acid sequence of Aglu-1 contains 902 amino acids with a predicted mass of 101 kD, including the putative signal sequence. The amino acid sequence of Aglu-1 is 42% to 48% identical to those of the recently reported cDNA clones from barley (Tibbot and Skadsen, 1996), spinach (Sugimoto et al, 1997), and sugar beet (Matsui et al, 1997). Although it is not completely sequenced, a second Arabidopsis gene, Aglu-2, known from six ESTs, is similar to Aglu-1 and each of the other plant ␣-glucosidases.…”

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confidence: 56%

“…In Arabidopsis there are at least three members of this family, two of which, Aglu-1 and Aglu-2, are as similar to each other as they are to other acidic ␣-glucosidases that have been cloned from barley (Tibbot and Skadsen, 1996), spinach (Sugimoto et al, 1997), and sugar beet (Matsui et al, 1997). A third more distantly related ␣-glucosidase gene, Aglu-3, is most similar to the ER glucosidase II, which catalyzes the hydrolysis of ␣-1,3-linked Glc from glycoproteins as they fold.…”

Section: The Aglu Gene Familymentioning

confidence: 99%

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Structure, Properties, and Tissue Localization of Apoplastic α-Glucosidase in Crucifers1

et al. 1999

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Apoplastic ␣-glucosidases occur widely in plants but their function is unknown because appropriate substrates in the apoplast have not been identified. Arabidopsis contains at least three ␣-glucosidase genes; Aglu-1 and Aglu-3 are sequenced and Aglu-2 is known from six expressed sequence tags. Antibodies raised to a portion of Aglu-1 expressed in Escherichia coli recognize two proteins of 96 and 81 kD, respectively, in vegetative tissues of Arabidopsis, broccoli (Brassica oleracea L.), and mustard (Brassica napus L.). The acidic ␣-glucosidase activity from broccoli flower buds was purified using concanavalin A and ion-exchange chromatography. Two active fractions were resolved and both contained a 96-kD immunoreactive polypeptide. The N-terminal sequence from the 96-kD broccoli ␣-glucosidase indicated that it corresponds to the Arabidopsis Aglu-2 gene and that approximately 15 kD of the predicted N terminus was cleaved. The 81-kD protein was more abundant than the 96-kD protein, but it was not active with 4-methylumbelliferyl-␣-D-glucopyranoside as the substrate and it did not bind to concanavalin A. In situ activity staining using 5-bromo-4-chloro-3-indolyl-␣-D-glucopyranoside revealed that the acidic ␣-glucosidase activity is predominantly located in the outer cortex of broccoli stems and in vascular tissue, especially in leaf traces.

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confidence: 56%

Section: The Aglu Gene Familymentioning

confidence: 99%

Structure, Properties, and Tissue Localization of Apoplastic α-Glucosidase in Crucifers1

et al. 1999

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“…A role in pathogen resistance has also been suggested and is discussed in Monroe's paper (Monroe et al 1999). The a-glucosidase sequences most closely related to the nasturtium a-D-xylosidase, Aglu1 from Arabidopsis (Monroe et al 1999), barley (Tibbot and Skadsen 1996), spinach (Sugimoto et al 1997) and sugar beet (Matsui et al 1997) all have deduced amino acid sequences of over 100 kDa. Furthermore the cDNAs of these proteins all have putative signal sequences and all appear to undergo post-translational modi®cation such as glycosylation and/or proteolysis (Monroe et al 1999).…”

Section: Discussionmentioning

confidence: 99%

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

Crombie

Chengappa

Jarman

et al. 2001

Planta

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We report the isolation, sequencing and analysis of the cDNA corresponding to an alpha-D-xylosidase involved in the mobilisation of xyloglucan from the cotyledons of germinated nasturtium (Tropaeolum majus L.) seeds. The translated open reading frame (2,808 bp including the stop codon), gave a polypeptide of 935 amino acids. It included the sequences of eleven peptides obtained by endo-proteinase digestion of the protein, and a putative hydrophobic signal sequence characteristic of a protein that is directed through the plasma membrane. The deduced molecular weight of the translated protein was appreciably higher than the molecular weight determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis, suggesting post-translational modification. The protein sequence showed high homology (76.0% identity over 896 amino acids) with a putative alpha-xylosidase sequence from Arabidopsis thaliana and there was homology with several alpha-glucosidases, notably those associated with the plant cell apoplast. The enzyme is a member of Family 31 of the glycosyl hydrolases and it fits into Clade 1 of the phylogenic analysis of alpha-glucosidases. Although in vivo the nasturtium enzyme catalyses mobilisation of cell wall xyloglucan, the homology of its primary sequence with alpha-glucosidases prompted study of its action on a range of alpha-glucosides. It was active against several alpha-(1-->4)-and alpha-(1-->6)-linked substrates, the former being hydrolysed faster. The functional and evolutionary relationships between this alpha-D-xylosidase and plant "apoplastic" alpha-D-glucosidases are discussed.

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“…Some of the α‐glucosidases are able to degrade soluble starch, viz . sugar beet α‐glucosidase (Chiba 1997; Matsui et al . 1997).…”

Section: Discussionmentioning

confidence: 99%

Purification and characterization of an extracellular alpha-glucosidase protein from Trichoderma viride which degrades a phytotoxin associated with sheath blight disease in rice

et al. 2001

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Aims: To purify and characterize an extracellular a-glucosidase from Trichoderma viride capable of inactivating a host-speci®c phytotoxin, designated RS toxin, produced by the rice sheath blight pathogen, Rhizoctonia solani Ku Èhn. Methods and Results: The host-speci®c RS toxin was puri®ed from both culture ®ltrates (culture ®ltrate toxin, CFTox) and R. solani-inoculated rice sheaths (sheath blight toxin, SBTox). Sodium dodecyl sulphate-polyacrylamide gel electrophoresis analyses of extracellular proteins, puri®ed from a biocontrol fungus T. viride (TvMNT7) grown on SBTox and CFTox separately, were carried out. The antifungal activity of the puri®ed high molecular weight protein (110 kDa) was studied against RS toxin as well as on the sclerotial germination and mycelial growth of R. solani. Enzyme assay and Western blot analysis with the antirabbit TvMNT7 110-kDa protein indicated that the protein was an a-glucosidase. The 110-kDa protein was highly speci®c to RS toxin and its Michaelis±Menten constant value was 0á40 mmol l )1 when p-nitrophenyl a-D D-glucopyranoside was used as the substrate. The isoelectric point of the protein was 5á2. N-terminal sequencing of the a-glucosidase protein showed that its amino acid sequence showed no homology with other known a-glucosidases.Conclusions: This appears to be the ®rst report of the puri®cation and characterization of an a-glucosidase capable of inactivating a host-speci®c toxin of fungal origin. The a-glucosidase is speci®c to RS toxin and is different from the known a-glucosidases. Signi®cance and Impact of the Study: As RS toxin could be inactivated by the microbial a-glucosidase enzyme, isolation of the gene that codes for the enzyme from T. viride and transfer of the gene to rice plants would lead to enhanced resistance against sheath blight pathogen by inactivation of RS toxin.

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Cloning and Sequencing of a cDNA Encoding α-Glucosidase from Sugar Beet

Cited by 21 publications

References 4 publications

Structure, Properties, and Tissue Localization of Apoplastic α-Glucosidase in Crucifers1

Structure, Properties, and Tissue Localization of Apoplastic α-Glucosidase in Crucifers1

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

Purification and characterization of an extracellular alpha-glucosidase protein from Trichoderma viride which degrades a phytotoxin associated with sheath blight disease in rice

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