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Publications - Cell and Metabolic Biology

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Publications

Van Damme, E. J. M.; Hause, B.; Hu, J.; Barre, A.; Rougé, P.; Proost, P.; Peumans, W. J.; 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 Plant Physiol. 130, 757-769, (2002) DOI: 10.1104/pp.005892

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.
Publications

Chen, Y.; Peumans, W. J.; Hause, B.; Bras, J.; Kumar, M.; Proost, P.; Barre, A.; Rougé, P.; Van Damme, E. J. M.; Jasmonate methyl ester induces the synthesis of a cytoplasmic/nuclear chitooligosaccharide‐binding lectin in tobacco leaves FASEB J. 16, 905-907, (2002) DOI: 10.1096/fj.01-0598fje

In contrast to animal lectins, no evidence has indicated the occurrence of plant lectins, which recognize and bind “endogenous” receptors and accordingly are involved in recognition mechanisms within the organism itself. Here we show that the plant hormone jasmonic acid methyl ester (JAME) induces in leaves of Nicotiana tabacum (var. Samsun NN) the expression of a lectin that is absent from untreated plants. The lectin specifically binds to oligomers of N‐acetylglucosamine and is detected exclusively in the cytoplasm and the nucleus. Both the subcellular location and specificity indicate that the Nicotiana tabacum agglutinin (called Nictaba) may be involved in the regulation of gene expression in stressed plants through specific protein‐carbohydrate interactions with regulatory cytoplasmic/nuclear glycoproteins. Searches in the databases revealed that many flowering plants contain sequences encoding putative homologues of the tobacco lectin, which suggest that Nictaba is the prototype of a widespread or possibly ubiquitous family of lectins with a specific endogenous role.
Publications

Hao, Q.; Van Damme, E. J. M.; Hause, B.; Barre, A.; Chen, Y.; Rougé, P.; Peumans, W. J.; Iris Bulbs Express Type 1 and Type 2 Ribosome-Inactivating Proteins with Unusual Properties Plant Physiol. 125, 866-876, (2001) DOI: 10.1104/pp.125.2.866

Two closely related lectins from bulbs of the Dutch iris (Iris hollandica var. Professor Blaauw) have been isolated and cloned. Both lectins, called Iris agglutinin b and Iris agglutinin r, possess N-glycosidase activity and share a high sequence similarity with previously described type 2 ribosome-inactivating proteins (RIP). However, these lectins show only 57% to 59% sequence identity to a previously characterized type 1 RIP from iris, called IRIP. The identification of the iris lectins as type 2 RIP provides unequivocal evidence for the simultaneous occurrence of type 1 and type 2 RIP in iris bulbs and allowed a detailed comparison of type 1 and type 2 RIP from a single plant, which provides further insight into the molecular evolution of RIP. Binding studies and docking experiments revealed that the lectins exhibit binding activity not only toward Gal/N-acetylgalactosamine, but also toward mannose, demonstrating for the first time that RIP-binding sites can accommodate mannose.
Publications

Van Damme, E. J. M.; Hu, J.; Barre, A.; Hause, B.; Baggerman, G.; Rougé, P.; Peumans, W. J.; Purification, characterization, immunolocalization and structural analysis of the abundant cytoplasmic β-amylase from Calystegia sepium (hedge bindweed) rhizomes Eur. J. Biochem. 268, 6263-6273, (2001) DOI: 10.1046/j.0014-2956.2001.02584.x

An abundant catalytically active β‐amylase (EC 3.2.1.2) was isolated from resting rhizomes of hedge bindweed (Calystegia sepium ). Biochemical analysis of the purified protein, molecular modeling, and cloning of the corresponding gene indicated that this enzyme resembles previously characterized plant β‐amylases with regard to its amino‐acid sequence, molecular structure and catalytic activities. Immunolocalization demonstrated that the β‐amylase is exclusively located in the cytoplasm. It is suggested that the hedge bindweed rhizome β‐amylase is a cytoplasmic vegetative storage protein.
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