Potato lectin: A three-domain glycoprotein with novel hydroxyproline-containing sequences and sequence similarities to wheat-germ agglutinin

A K Allen, G P Bolwell, David Stanley Brown, C Sidebottom, A R Slabas

    Research output: Contribution to journalArticle

    32 Citations (Scopus)

    Abstract

    Potato (Solanum tuberosum) tuber lectin is a chitin-binding, hydroxyproline-rich glycoprotein, which may be involved in the defence mechanisms of the plant. We had previously obtained evidence that it consists of at least two very dissimilar domains. The aim was to use a combination of accurate determinations of molecular weight and protein sequencing to gain more accurate information on the domains. Accurate determinations of the molecular weight of the lectin by a MALDI mass spectrometer have shown that the subunit molecular weight is 65500 ( +/- 1100) and that of a totally deglycosylated sample is 31250 (+/- 30). This means that the lectin is 52.3(+/- 1)% carbohydrate with a considerable number of glycoforms being present. Partial sequences rind other analyses are consistent with the existence of three distinct domains. These are: (1) air N-terminal region which is rich in proline but poor in hydroxyproline; (2) a glycosylated region with a glycosylated molecular weight of 45300 (+/- 1100) and a deglycosylated molecular weight of 11050 (+/- 50) which is extremely rich in glycosylated hydroxyproline residues with a similar sequence to extensins; and (3) a cystine-rich domain which has the sugar binding site shows partial conservation of a repeated moth common to many chitin-binding proteins of the hevin family including wheat-germ agglutinin. The closest similarity seems to be to the sequence of potato basic chitinase. Copyright (C) 1996 Elsevier Science Ltd

    Original languageEnglish
    Pages (from-to)1285-1291
    Number of pages7
    JournalInternational Journal of Biochemistry & Cell Biology
    Volume28
    Issue number11
    DOIs
    Publication statusPublished - Nov 1996

    Keywords

    • potato lectin
    • (Solanum tuberosum)
    • protein sequences
    • hydroxyproline-rich glycoprotein
    • chitin binding
    • MALDI mass spectrometry
    • solanum-tuberosum lectin
    • chitin-binding proteins
    • trifluoromethane sulfonic acid
    • extracellular-matrix
    • purification
    • extensin
    • deglycosylation
    • isolectin
    • family
    • genes

    Cite this

    Potato lectin: A three-domain glycoprotein with novel hydroxyproline-containing sequences and sequence similarities to wheat-germ agglutinin. / Allen, A K ; Bolwell, G P ; Brown, David Stanley; Sidebottom, C ; Slabas, A R .

    In: International Journal of Biochemistry & Cell Biology, Vol. 28, No. 11, 11.1996, p. 1285-1291.

    Research output: Contribution to journalArticle

    Allen, A K ; Bolwell, G P ; Brown, David Stanley ; Sidebottom, C ; Slabas, A R . / Potato lectin: A three-domain glycoprotein with novel hydroxyproline-containing sequences and sequence similarities to wheat-germ agglutinin. In: International Journal of Biochemistry & Cell Biology. 1996 ; Vol. 28, No. 11. pp. 1285-1291.
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    abstract = "Potato (Solanum tuberosum) tuber lectin is a chitin-binding, hydroxyproline-rich glycoprotein, which may be involved in the defence mechanisms of the plant. We had previously obtained evidence that it consists of at least two very dissimilar domains. The aim was to use a combination of accurate determinations of molecular weight and protein sequencing to gain more accurate information on the domains. Accurate determinations of the molecular weight of the lectin by a MALDI mass spectrometer have shown that the subunit molecular weight is 65500 ( +/- 1100) and that of a totally deglycosylated sample is 31250 (+/- 30). This means that the lectin is 52.3(+/- 1){\%} carbohydrate with a considerable number of glycoforms being present. Partial sequences rind other analyses are consistent with the existence of three distinct domains. These are: (1) air N-terminal region which is rich in proline but poor in hydroxyproline; (2) a glycosylated region with a glycosylated molecular weight of 45300 (+/- 1100) and a deglycosylated molecular weight of 11050 (+/- 50) which is extremely rich in glycosylated hydroxyproline residues with a similar sequence to extensins; and (3) a cystine-rich domain which has the sugar binding site shows partial conservation of a repeated moth common to many chitin-binding proteins of the hevin family including wheat-germ agglutinin. The closest similarity seems to be to the sequence of potato basic chitinase. Copyright (C) 1996 Elsevier Science Ltd",
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    T1 - Potato lectin: A three-domain glycoprotein with novel hydroxyproline-containing sequences and sequence similarities to wheat-germ agglutinin

    AU - Allen, A K

    AU - Bolwell, G P

    AU - Brown, David Stanley

    AU - Sidebottom, C

    AU - Slabas, A R

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    N2 - Potato (Solanum tuberosum) tuber lectin is a chitin-binding, hydroxyproline-rich glycoprotein, which may be involved in the defence mechanisms of the plant. We had previously obtained evidence that it consists of at least two very dissimilar domains. The aim was to use a combination of accurate determinations of molecular weight and protein sequencing to gain more accurate information on the domains. Accurate determinations of the molecular weight of the lectin by a MALDI mass spectrometer have shown that the subunit molecular weight is 65500 ( +/- 1100) and that of a totally deglycosylated sample is 31250 (+/- 30). This means that the lectin is 52.3(+/- 1)% carbohydrate with a considerable number of glycoforms being present. Partial sequences rind other analyses are consistent with the existence of three distinct domains. These are: (1) air N-terminal region which is rich in proline but poor in hydroxyproline; (2) a glycosylated region with a glycosylated molecular weight of 45300 (+/- 1100) and a deglycosylated molecular weight of 11050 (+/- 50) which is extremely rich in glycosylated hydroxyproline residues with a similar sequence to extensins; and (3) a cystine-rich domain which has the sugar binding site shows partial conservation of a repeated moth common to many chitin-binding proteins of the hevin family including wheat-germ agglutinin. The closest similarity seems to be to the sequence of potato basic chitinase. Copyright (C) 1996 Elsevier Science Ltd

    AB - Potato (Solanum tuberosum) tuber lectin is a chitin-binding, hydroxyproline-rich glycoprotein, which may be involved in the defence mechanisms of the plant. We had previously obtained evidence that it consists of at least two very dissimilar domains. The aim was to use a combination of accurate determinations of molecular weight and protein sequencing to gain more accurate information on the domains. Accurate determinations of the molecular weight of the lectin by a MALDI mass spectrometer have shown that the subunit molecular weight is 65500 ( +/- 1100) and that of a totally deglycosylated sample is 31250 (+/- 30). This means that the lectin is 52.3(+/- 1)% carbohydrate with a considerable number of glycoforms being present. Partial sequences rind other analyses are consistent with the existence of three distinct domains. These are: (1) air N-terminal region which is rich in proline but poor in hydroxyproline; (2) a glycosylated region with a glycosylated molecular weight of 45300 (+/- 1100) and a deglycosylated molecular weight of 11050 (+/- 50) which is extremely rich in glycosylated hydroxyproline residues with a similar sequence to extensins; and (3) a cystine-rich domain which has the sugar binding site shows partial conservation of a repeated moth common to many chitin-binding proteins of the hevin family including wheat-germ agglutinin. The closest similarity seems to be to the sequence of potato basic chitinase. Copyright (C) 1996 Elsevier Science Ltd

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    KW - trifluoromethane sulfonic acid

    KW - extracellular-matrix

    KW - purification

    KW - extensin

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    KW - family

    KW - genes

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    SN - 1357-2725

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    ER -