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BIOCHEMICAL PROCESSES AND MACROMOLECULAR STRUCTURES

Characterization of Synthetic Hydroxyproline-Rich Proteoglycans with Arabinogalactan Protein and Extensin Motifs in Arabidopsis^1,[W]

Department of Plant Biology, Carnegie Institution, Stanford, California 94305 (J.M.E., N.K., C.S.); Department of Chemistry and Biochemistry, Ohio University, Athens, Ohio 45701 (M.J.K.); and Department of Biological Sciences, Stanford University, Stanford, California 94305 (C.S.)

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 (Arabidopsis thaliana) under the 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 in roots. The amount of hydroxylation and glycosylation of the various constructs varied depending on the tissue. Also, accumulation of the proteins exhibited a high degree of cell-type specificity within various tissues due to posttranscriptional effects. The observations reveal a high level of complexity in the synthesis, secretion, and turnover of the glycoproteins.

The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Chris Somerville (crs{at}stanford.edu).

^[W] The online version of this article contains Web-only data.

www.plantphysiol.org/cgi/doi/10.1104/pp.106.084244

^* Corresponding author; e-mail crs{at}stanford.edu; fax 650–325–6857.

Received May 26, 2006; accepted August 20, 2006; published August 25, 2006.

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