Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Plant Physiology 86:922-926 (1988)
© 1988 American Society of Plant Biologists

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Metabolism and Enzymology

Biosynthesis of the Snowdrop (Galanthus nivalis) Lectin in Ripening Ovaries 1

Els J. M. Van Damme and Willy J. Peumans

Laboratorium voor Plantenbiochemie, Facultein der Landbouwwetenschappen, Willem de Croylaan 42, B-3030 Leuven, Belgium

The biosynthesis and processing of the Galanthus nivalis agglutinin were studied in vivo in ripening snowdrop ovaries. Using labeling and pulse chase labeling experiments it could be demonstrated that the snowdrop lectin is synthesized as a precursor of relative molecular weight (Mr) 15,000 which is posttranslationally converted into the authentic lectin polypeptide of Mr 13,000 with a half-life of about 6 hours. Gel filtration of an extract of [3H]leucine labeled ovaries on Sepharose 4B showed that a significant portion of the newly synthesized lectin is associated with the particulate fraction. When the organellar fraction was fractionated on isopycnic sucrose gradients this lectin banded in the same density region as the endoplasmic reticulum (ER) marker enzyme NADH cytochrome c reductase. Both radioactivity in lectin and in enzyme activity shifted towards a higher density in the presence of 2 millimolar Mg-acetate indicating that the labeled lectin was associated with the rough ER. Labeled lectin could be chased from the ER with a half-life of 4 hours and then accumulated in the soluble fraction. Whereas the ER-associated lectin contains exclusively polypeptides of Mr 15,000 the soluble fraction contains both precursor molecules and mature lectin polypeptides. The snowdrop lectin in the ER is fully capable of binding immobilized mannose. It is associated into tetramers with an appropriate molecular weight of 60,000. These results indicate that newly synthesized snowdrop lectin is transiently associated with the ER before transport and processing.

1 Supported in part by grants of the National Fund for Scientific Research (Belgium) of which W. P. is a Senior Research Associate. E. V. D. acknowledges the receipt of a Fellowship of the Belgian Instituut tot Aanmoediging van het Wetenschappelijk Onderzoek in Nijverheid en Landbouw.




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E. Fouquaert, S. L. Hanton, F. Brandizzi, W. J. Peumans, and E. J. M. Van Damme
Localization and Topogenesis Studies of Cytoplasmic and Vacuolar Homologs of the Galanthus nivalis Agglutinin
Plant Cell Physiol., July 1, 2007; 48(7): 1010 - 1021.
[Abstract] [Full Text] [PDF]


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