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THE PLANT CELL, Vol 7, Issue 9 1459-1471, Copyright © 1995 by American Society of Plant Biologists
Plant Nuclear Pore Complex Proteins Are Modified by Novel Oligosaccharides with Terminal N-Acetylglucosamine
A. Heese-Peck, R. N. Cole, O. N. Borkhsenious, G. W. Hart and N. V. Raikhel
Michigan State University-Department of Energy Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824-1312
Only a few nuclear pore complex (NPC) proteins, mainly in vertebrates and
yeast but none in plants, have been well characterized. As an initial step
to identify plant NPC proteins, we examined whether NPC proteins from
tobacco are modified by N-acetylglucosamine (GlcNAc). Using wheat germ
agglutinin, a lectin that binds specifically to GlcNAc in plants, specific
labeling was often found associated with or adjacent to NPCs. Nuclear
proteins containing GlcNAc can be partially extracted by 0.5 M salt, as
shown by a wheat germ agglutinin blot assay, and at least eight extracted
proteins were modified by terminal GlcNAc, as determined by in vitro
galactosyltransferase assays. Sugar analysis indicated that the plant
glycans with terminal GlcNAc differ from the single O-linked GlcNAc of
vertebrate NPC proteins in that they consist of oligosaccharides that are
larger in size than five GlcNAc residues. Most of these appear to be bound
to proteins via a hydroxyl group. This novel oligosaccharide modification
may convey properties to the plant NPC that are different from those of
vertebrate NPCs.
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