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J. Biol. Chem., Vol. 279, Issue 44, 45503-45511, October 29, 2004

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Post-translational Modifications of Arabinogalactan-peptides of Arabidopsis thaliana

ENDOPLASMIC RETICULUM AND GLYCOSYLPHOSPHATIDYLINOSITOL-ANCHOR SIGNAL CLEAVAGE SITES AND HYDROXYLATION OF PROLINE^*

Carolyn J. Schultz, Kris L. Ferguson¶||, Jelle Lahnstein||, and Antony Bacic¶

From the School of Agriculture and Wine, Waite Agricultural Research Institute, The University of Adelaide, PMB1, Glen Osmond, South Australia 5064, Australia and the ^¶Australian Centre for Plant Functional Genomics and Plant Cell Biology Research Centre, School of Botany, The University of Melbourne, Parkville, Victoria, 3010 Australia

We have developed a method for separating the deglycosylated protein/peptide backbones of the small arabinogalactan (AG)-peptides from the larger classical arabinogalactan-proteins (AGPs). AGPs are an important class of plant proteoglycans implicated in plant growth and development. Separation of AG-peptides enabled us to identify eight of 12 AG-peptides from Arabidopsis thaliana predicted from genomic sequences. Of the remaining four, two have low abundance based on expressed sequence tag databases and the other two are only present in pollen (At3g20865) or flowers (At3g57690) and therefore would not be detected in our analysis. Characterization of AG-peptides was performed using matrix-assisted laser desorption ionization-time of flight mass spectrometry and tandem mass spectrometry protein sequencing. These data provide (i) experimental evidence that AG-peptides are processed in vivo for the addition of a glycosylphosphatidylinositol (GPI) anchor, (ii) cleavage site information for both the endoplasmic reticulum secretion signal and the GPI-anchor signal for eight of the 12 AG-peptides, and (iii) experimental evidence that the Gly-Pro motif is hydroxylated in vivo. Furthermore, we show that AtAGP16 is GPI-anchored despite its unusually long hydrophobic C-terminal GPI-signal sequence. Prior to this work, the GPI-anchor cleavage site for only two plant proteins, NaAGP1 from Nicotiana alata and PcAGP1 from Pyrus communis, had been determined experimentally. Characterization of the post-translational modifications of AG-peptides contributes toward obtaining the complete primary structure of this class of biologically important plant proteoglycans and provides a greater understanding of post-translational modifications of plant proteins.

Received for publication, July 7, 2004 , and in revised form, August 16, 2004.

^* This work was supported in part by Australian Research Council Grants A10020017 and DP0343454 (to A. B. and C. S.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Tables IV, V, and VI and Fig. 4.

^|| Supported by Australian Research Council and Grains and Development Research and Development Corporation grant to the Australian Centre for Plant Functional Genomics.

To whom correspondence should be addressed. Tel.: 61-8-8303-7342; Fax: 61-8-8303-7109; E-mail: carolyn.schultz{at}adelaide.edu.au.

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