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Carbohydrate Modifications of the High Mobility Group Proteins
Raymond Reeves, David Chang and Shu-Ching Chung
Proceedings of the National Academy of Sciences of the United States of America
Vol. 78, No. 11, [Part 2: Biological Sciences] (Nov., 1981), pp. 6704-6708
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/11332
Page Count: 5
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This paper reports the results of numerous biochemical analyses which indicate that the ``high mobility group'' proteins (HMGs) of mouse and bovine cells are bona fide glycoproteins and can, in addition, be modified by poly(ADP-ribose) addition in vitro. The sugars N-acetylglucosamine, mannose, galactose, glucose, fucose, and one unknown sugar (possibly xylose) have been identified in purified preparations of HMGs 14 and 17. Furthermore, the fucose-specific lectin Ulex europeus agglutinin I bound both to the isolated HMGs and to monomer nucleosomes containing HMGs released from ``active chromatin'' by micrococcal nuclease digestion. Selective alkaline borohydride reductive cleavages of the HMGs suggested that the oligosaccharide prosthetic groups are primarily bound to these proteins by N-glycosidic linkages. The unexpected finding that the HMGs contain covalently bound complex carbohydrate moieties allows for a potentially great amount of variability and specificity in these proteins that may have important biological implications.
Proceedings of the National Academy of Sciences of the United States of America © 1981 National Academy of Sciences