The liverwort contains a lectin that is structurally and evolutionary related to the monocot mannose-binding lectins. Peumans, W., J., Barre, A., Bras, J., Rougé, P., Proost, P., & Van Damme, E., J., M. Plant Physiology, 129(3):1054-1065, American Society of Plant Physiologists, 2002. abstract bibtex A mannose (Man)-binding lectin has been isolated and characterized from the thallus of the liverwort Marchantia polymorpha. N-terminal sequencing indicated that the M. polymorpha agglutinin (Marpola) shares sequence similarity with the superfamily of monocot Man-binding lectins. Searches in the databases yielded expressed sequence tags encoding Marpola. Sequence analysis, molecular modeling, and docking experiments revealed striking structural similarities between Marpola and the monocot Man-binding lectins. Activity and specificity studies further indicated that Marpola is a much stronger agglutinin than the Galanthus nivalis agglutinin and exhibits a preference for methylated Man and glucose, which is unprecedented within the family of monocot Man-binding lectins. The discovery of Marpola allows us, for the first time, to corroborate the evolutionary relationship between a lectin from a lower plant and a well-established lectin family from flowering plants. In addition, the identification of Marpola sheds a new light on the molecular evolution of the superfamily of monocot Man-binding lectins. Beside evolutionary considerations, the occurrence of a G. nivalis agglutinin homolog in a lower plant necessitates the rethinking of the physiological role of the whole family of monocot Man-binding lectins.
@article{
title = {The liverwort contains a lectin that is structurally and evolutionary related to the monocot mannose-binding lectins.},
type = {article},
year = {2002},
pages = {1054-1065},
volume = {129},
publisher = {American Society of Plant Physiologists},
institution = {Laboratory for Phytopathology and Plant Protection, Rega Institute, Katholieke Universiteit Leuven, 3001 Leuven, Belgium.},
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abstract = {A mannose (Man)-binding lectin has been isolated and characterized from the thallus of the liverwort Marchantia polymorpha. N-terminal sequencing indicated that the M. polymorpha agglutinin (Marpola) shares sequence similarity with the superfamily of monocot Man-binding lectins. Searches in the databases yielded expressed sequence tags encoding Marpola. Sequence analysis, molecular modeling, and docking experiments revealed striking structural similarities between Marpola and the monocot Man-binding lectins. Activity and specificity studies further indicated that Marpola is a much stronger agglutinin than the Galanthus nivalis agglutinin and exhibits a preference for methylated Man and glucose, which is unprecedented within the family of monocot Man-binding lectins. The discovery of Marpola allows us, for the first time, to corroborate the evolutionary relationship between a lectin from a lower plant and a well-established lectin family from flowering plants. In addition, the identification of Marpola sheds a new light on the molecular evolution of the superfamily of monocot Man-binding lectins. Beside evolutionary considerations, the occurrence of a G. nivalis agglutinin homolog in a lower plant necessitates the rethinking of the physiological role of the whole family of monocot Man-binding lectins.},
bibtype = {article},
author = {Peumans, Willy J and Barre, Annick and Bras, Julien and Rougé, Pierre and Proost, Paul and Van Damme, Els J M},
journal = {Plant Physiology},
number = {3}
}
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