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THE PLANT CELL, Vol 6, Issue 11 1643-1653, Copyright © 1994 by American Society of Plant Biologists
Isolation of the Protein Backbone of an Arabinogalactan-Protein from the Styles of Nicotiana alata and Characterization of a Corresponding cDNA
H. Du, R. J. Simpson, R. L. Moritz, A. E. Clarke and A. Bacic
Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Parkville, Victoria 3052, Australia
Arabinogalactan-proteins (AGPs) from the styles of Nicotiana alata were
isolated by ion exchange and gel filtration chromatography. After
deglycosylation by anhydrous hydrogen fluoride, the protein backbones were
fractionated by reversed-phase HPLC. One of the protein backbones,
containing mainly hydroxyproline, alanine, and serine residues (53% of
total residues), was digested with proteases, and the peptides were
isolated and sequenced. This sequence information allowed the cloning of a
712-bp cDNA, AGPNa1. AGPNa1 encodes a 132-amino acid protein with three
domains: an N-terminal secretion signal sequence, which is cleaved from the
mature protein; a central sequence, which contains most of the
hydroxyproline/proline residues; and a C-terminal hydrophobic region.
AGPNa1 is expressed in many tissues of N. alata and related species. The
arrangement of domains and amino acid composition of the AGP encoded by
AGPNa1 are similar to that of an AGP from pear cell suspension culture
filtrate, although the only sequence identity is at the N termini of the
mature proteins.
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