دورية أكاديمية
Calcium modulates protease resistance and carbohydrate binding of a plant defense legume lectin, Griffonia simplicifolia lectin II (GSII).
| العنوان: | Calcium modulates protease resistance and carbohydrate binding of a plant defense legume lectin, Griffonia simplicifolia lectin II (GSII). |
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| المؤلفون: | Zhu-Salzman K; Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA. ksalzman@tamu.edu, Hammen PK, Salzman RA, Koiwa H, Bressan RA, Murdock LL, Hasegawa PM |
| المصدر: | Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology [Comp Biochem Physiol B Biochem Mol Biol] 2002 Jun; Vol. 132 (2), pp. 327-34. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: Pergamon Country of Publication: England NLM ID: 9516061 Publication Model: Print Cited Medium: Print ISSN: 1096-4959 (Print) Linking ISSN: 10964959 NLM ISO Abbreviation: Comp Biochem Physiol B Biochem Mol Biol Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Oxford : Pergamon Original Publication: Oxford : Tarrytown, NY : Pergamon ; Elsevier, c1994- |
| مواضيع طبية MeSH: | Carbohydrate Metabolism*, Calcium/*pharmacology , Griffonia/*drug effects , Griffonia/*metabolism , Papain/*metabolism , Plant Lectins/*metabolism, Animals ; Binding Sites ; Circular Dichroism ; Griffonia/genetics ; Insecta/enzymology ; Plant Lectins/genetics ; Point Mutation ; Protein Binding/drug effects ; Protein Folding ; Urea/pharmacology |
| مستخلص: | Site-directed mutagenesis previously identified the residues responsible for the biological activity of the plant defense legume lectin, Griffonia simplicifolia lectin II (GSII) [Proc. Natl. Acad. Sci. USA 95, (1998) 15123-15128]. However, these results were inconclusive as to whether these residues function as direct defense determinants through carbohydrate binding, or whether substantial changes of the protein structure had occurred in mutated proteins, with this structural disruption actually causing the loss of biochemical and biological functions. Evidence shown here supports the former explanation: circular dichroism and fluorescence spectra showed that mutations at carbohydrate-binding residues of GSII do not render it dysfunctional because of substantial secondary or tertiary structure modifications; and trypsin treatment confirmed that rGSII structural integrity is retained in these mutants. Reduced biochemical stability was observed through papain digestion and urea denaturation in mutant versions that had lost carbohydrate-binding ability, and this was correlated with lower Ca(2+) content. Accordingly, the re-addition of Ca(2+) to demetalized proteins could recover resistance to papain in the carbohydrate-binding mutant, but not in the non-binding mutant. Thus, both carbohydrate binding (presumably to targets in the insect gut) and biochemical stability to proteolytic degradation in situ indeed contribute to anti-insect activity, and these activities are Ca(2+)-dependent. |
| المشرفين على المادة: | 0 (Plant Lectins) 8W8T17847W (Urea) EC 3.4.22.2 (Papain) SY7Q814VUP (Calcium) |
| تواريخ الأحداث: | Date Created: 20020529 Date Completed: 20030103 Latest Revision: 20190916 |
| رمز التحديث: | 20240829 |
| DOI: | 10.1016/s1096-4959(02)00033-7 |
| PMID: | 12031457 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1096-4959 |
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| DOI: | 10.1016/s1096-4959(02)00033-7 |