A cDNA corresponding to the core protein of an immunoaffinity-purified arabinogalactan protein (AGP) secreted by Daucus carota (carrot) cells in liquid culture was isolated. This cDNA, DcAGP1, encodes a new class of `non-classical' AGP with strong similarity to a family of basic proline-rich proteins. The protein is rich in proline (17%), alanine (10%) and lysine (11%) and contains four distinct domains: a signal peptide, a proline-rich domain, a histidine-rich basic domain and a cysteine-containing `PAC' domain that is found in a range of other cell wall proteins. The protein contains several sequence motifs found in otherwise unrelated cell wall proteins, but also displays some unique features. Northern blot analyses show that while the DcAGP1 transcript is abundant in the suspension-culture cells from which the AGP was obtained; in carrot seedlings the gene is only expressed at low levels in the roots and it is neither wound- nor stress-inducible. Furthermore, northern and western blot analyses demonstrate that the core polypeptide of DcAGP1 is differentially glycosylated in two different carrot suspension cultures. The unusual features of the protein sequence suggest that the DcAGP1 protein is a member of a family of basic proline-rich proteins defined by the C-terminal PAC domain, and the possible function(s) of the DcAGP1 protein is considered in the light of current views on AGP structure and function.
Plant Molecular Biology – Springer Journals
Published: Oct 4, 2004
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