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Published on August 25, 2006; 10.1104/pp.106.084244

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Received May 26, 2006
Accepted August 20, 2006

Characterization of synthetic hydroxyproline-rich proteoglycans with AGP- and extensin-motifs in Arabidopsis

José M. Estévez , Marcia J. Kieliszewski , Natalie Khitrov , and Chris Somerville *

Department of Plant Biology, Carnegie Institution, 260 Panama Street, Stanford, California 94305
Department of Chemistry and Biochemistry, Ohio University, Athens, Ohio 45701
Department of Plant Biology, Carnegie Institution, 260 Panama Street, Stanford, California 94305; Department of Biological Sciences, Stanford University

* Corresponding author; email: crs{at}stanford.edu.

A series of gene constructs encoding synthetic glycomodule peptides with N-terminal signal sequences and C-terminal green fluorescent proteins were expressed in transgenic Arabidopsis under control of the 35S promoter. The synthetic glycomodule peptides were composed of repetitive proline-containing motifs that have been previously found to be substrates for prolyl hydroxylases and subsequent O-glycosylation of the hydroxyproline residues. All of the constructs were secreted in aerial tissues but not secreted in roots. The amount of hydroxylation and glycosylation of the various constructs varied depending on the tissue. Also, the accumulation of the proteins exhibited a high degree of cell-type specificity within various tissues due to post-transcriptional effects. The observations reveal a high level of complexity in the synthesis, secretion, and turnover of the glycoproteins.




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