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Synthetic Genes for Glycoprotein Design and the Elucidation of Hydroxyproline-O-glycosylation Codes
Elena Shpak, Joseph F. Leykam and Marcia J. Kieliszewski
Proceedings of the National Academy of Sciences of the United States of America
Vol. 96, No. 26 (Dec. 21, 1999), pp. 14736-14741
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/121151
Page Count: 6
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Design of hydroxyproline (Hyp)-rich glycoproteins (HRGPs) offers an approach for the structural and functional analysis of these wall components, which are broadly implicated in plant growth and development. HRGPs consist of multiple small repetitive "glycomodules" extensively O-glycosylated through the Hyp residues. The patterns of Hyp-O-glycosylation are putatively coded by the primary sequence as described by the Hyp contiguity hypothesis, which predicts contiguous Hyp residues to be attachment sites of small arabinooligosaccharides (1-5 Ara residues/Hyp); while clustered, noncontiguous Hyp residues are sites of arabinogalactan polysaccharide attachment. As a test, we designed two simple HRGPs as fusion proteins with green fluorescent protein. The first was a repetitive Ser-Hyp motif that encoded only clustered non-contiguous Hyp residues, predicted polysaccharide addition sites. The resulting glycoprotein had arabinogalactan polysaccharide O-linked to all Hyp residues. The second construct, based on the consensus sequence of a gum arabic HRGP, contained both arabinogalactan and arabinooligosaccharide addition sites and, as predicted, gave a product that contained both saccharide types. These results identify an O-glycosylation code of plants.
Proceedings of the National Academy of Sciences of the United States of America © 1999 National Academy of Sciences