Complete Amino Acid Sequence of Japanese Chestnut Agglutinin

Nomura, Keiichi; Nakamura, Sachiko; Fujitake, Mihoyo; Nakanishi, Tetsu

doi:10.1006/bbrc.2000.3420

Cited by 30 publications

(32 citation statements)

References 24 publications

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“…seeds contain both lectin and seed storage proteins (SSP). Judging from its carbohydrate specificity, 20) and amino acid sequence, 21) it was found that Japanese chestnut agglutinin (CCA) belongs to the mannosebinding JRL family. In addition, since cDNA cloning demonstrated that CCA does not undergo posttranslational proteolysis, 22) CCA is assumed to be present in the cytoplasm.…”

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confidence: 99%

The Expression Profile of Lectin Differs from That of Seed Storage Proteins inCastanea crenataTrees

Nakamura

Ikegami

Mizuno

et al. 2004

Bioscience, Biotechnology, and Biochemistry

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confidence: 99%

The Expression Profile of Lectin Differs from That of Seed Storage Proteins inCastanea crenataTrees

Nakamura

Ikegami

Mizuno

et al. 2004

Bioscience, Biotechnology, and Biochemistry

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“…Jacalin, the prototype of JRLs, was isolated from seeds of jack fruit (Artocarpus integrifolia; Moraceae) (5). Subsequently, JRLs have also been isolated and characterized from various plant families of angiosperms such as Convolvulaceae (6), Asteraceae (7), Gramineae (8,9), Musaceae (10 -12), Fagaceae (13), and Mimosaceae (14). Although JRLs are widely distributed in higher plants, no information on JRLs outside of angiosperms is available except for a recently isolated lectin from the Japanese cycad (Cycas revoluta) of gymnosperm subdivision (15).…”

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Purification, Characterization, Molecular Cloning, and Expression of Novel Members of Jacalin-related Lectins from Rhizomes of the True Fern Phlebodium aureum (L) J. Smith (Polypodiaceae)

Tateno¹,

Winter

Petryniak

et al. 2003

Journal of Biological Chemistry

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A lectin was purified from rhizomes of the fern Phlebodium aureum by affinity chromatography on mannose-Sepharose. The lectin, designated P. aureum lectin (PAL), is composed of two identical subunits of ϳ15 kDa associated by noncovalent bonds. From a cDNA library and synthetic oligonucleotide probes based on a partial amino acid sequence, 5-and 3-rapid amplification of cDNA ends allowed the generation of two similar fulllength cDNAs, termed PALa and PALb, each of which had an open reading frame of 438 bp encoding 146 amino acid residues. The two proteins share 88% sequence identity and showed structural similarity to jacalin-related lectins. PALa contained peptide sequences exactly matching those found in the isolated lectin. PALa and PALb were expressed in Escherichia coli using pET22b(؉) vector and purified by one-step affinity chromatography. Native and recombinant forms of PAL agglutinated rabbit erythrocytes and precipitated with yeast mannan, dextran, and the high mannose-containing glycoprotein invertase. The detailed carbohydrate-binding properties of the native and recombinant lectins were elucidated by agglutination inhibition assay, and native lectin was also studied by isothermal titration calorimetry. Based on the results of these assays, we conclude that this primitive vascular plant, like many higher plants, contains significant quantities of a mannose/glucose-binding protein in its storage tissue, whose binding specificity differs in detail from either legume mannose/ glucose-binding lectins or monocot mannose-specific lectins. The identification of a jacalin-related lectin in a true fern reveals for the first time the widespread distribution and molecular evolution of this lectin family in the plant kingdom.Lectins are proteins (or glycoproteins), other than antibodies and enzymes, that bind specifically and reversibly to carbohydrates, resulting in cell agglutination or precipitation of polysaccharides and glycoconjugates (1). They are ubiquitous in the biosphere, having been found in viruses, bacteria, fungi, plants, and animals (2). Among the divisions of the plant kingdom, the Pteridophyta, which includes the class Filicinae, or true ferns, have been largely overlooked in the study of lectins.Lectins of known specificity serve as valuable reagents in glycobiological research. They can be employed for the detection and preliminary characterization of glycoconjugates on the surface of cells. Although many lectins belong to the same major specificity group of mannose-or mannose/glucose-binding lectins, their different reactivities toward more complex oligo-and polysaccharides render many of them specifically valuable for recognizing a particular type of saccharide structure and fuel the search for yet more novel lectins (3). Lectins are found in greatest quantity and are most readily purified from plant sources, especially storage tissues such as seeds, bark, bulbs, rhizomes, etc. Many lectins have been isolated and characterized from angiosperm subdivision of seed plants. On the basis of struc...

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“…They are synthesized and located in the cytoplasm and undergo no co-or posttranslational proteolytic modification (Peumans et al, 2000a). Man-specific JRLs have been isolated from species belonging to a wide range of taxonomic groups, including hedge bindweed (Calystegia sepium, family Convolvulaceae; Van Damme et al, 1996;Peumans et al, 1997), Jerusalem artichoke (Helianthus tuberosus, family Asteraceae; , jack fruit (Artocarpus integrifolia, Moraceae; Rosa et al, 1999), rice (Oryza sativa, family Gramineae; Zhang et al, 2000), banana (Musa acuminata, family Musaceae; Peumans et al, 2000b), Japanese chestnut (Castanea crenata, family Fagaceae; Nomura et al, 2000), Parkia platycephala (family Fabaceae; Mann et al, 2001), and oilseed rape (Brassica napus, Brassicacea) plants (Geshi and Brandt, 1998). At present, the exact relationships between the two subfamilies of JRLs are still unclear because thus far no detailed study was made of a Gal-and a Man-specific JRL from a single species.…”

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Two Distinct Jacalin-Related Lectins with a Different Specificity and Subcellular Location Are Major Vegetative Storage Proteins in the Bark of the Black Mulberry Tree

Damme

Hause

et al. 2002

Plant Physiology

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Using a combination of protein isolation/characterization and molecular cloning, we have demonstrated that the bark of the black mulberry tree (Morus nigra) accumulates large quantities of a galactose-specific (MornigaG) and a mannose (Man)-specific (MornigaM) jacalin-related lectin. MornigaG resembles jacalin with respect to its molecular structure, specificity, and co-and posttranslational processing indicating that it follows the secretory pathway and eventually accumulates in the vacuolar compartment. In contrast, MornigaM represents a novel type of highly active Man-specific jacalin-related lectin that is synthesized without signal peptide or other vacuolar targeting sequences, and accordingly, accumulates in the cytoplasm. The isolation and cloning, and immunocytochemical localization of MornigaG and MornigaM not only demonstrates that jacalin-related lectins act as vegetative storage proteins in bark, but also allows a detailed comparison of a vacuolar galactose-specific and a cytoplasmic Man-specific jacalin-related lectin from a single species. Moreover, the identification of MornigaM provides the first evidence, to our knowledge, that bark cells accumulate large quantities of a cytoplasmic storage protein. In addition, due to its high activity, abundance, and ease of preparation, MornigaM is of great potential value for practical applications as a tool and bioactive protein in biological and biomedical research.

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Complete Amino Acid Sequence of Japanese Chestnut Agglutinin

Cited by 30 publications

References 24 publications

The Expression Profile of Lectin Differs from That of Seed Storage Proteins inCastanea crenataTrees

The Expression Profile of Lectin Differs from That of Seed Storage Proteins inCastanea crenataTrees

Purification, Characterization, Molecular Cloning, and Expression of Novel Members of Jacalin-related Lectins from Rhizomes of the True Fern Phlebodium aureum (L) J. Smith (Polypodiaceae)

Two Distinct Jacalin-Related Lectins with a Different Specificity and Subcellular Location Are Major Vegetative Storage Proteins in the Bark of the Black Mulberry Tree

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