Purification and cloning of an arabinogalactan-protein from xylem of loblolly pine |
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Authors: | Carol A. Loopstra Jeffrey D. Puryear Eun-Gyu No |
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Affiliation: | (1) Department of Forest Science and Crop Biotechnology Center, Texas A&M University, MS 2123, College Station, TX 77843, USA, US |
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Abstract: | An arabinogalactan-protein (AGP) was purified from differentiating xylem of loblolly pine (Pinus taeda L.) and the N-terminal sequence used to identify a cDNA clone. The protein, PtaAGP3, was not coded for by any previously identified AGP-like genes. Moreover, PtaAGP3 was abundantly and preferentially expressed in differentiating xylem. The encoded protein contains four domains, a signal peptide, a cleaved hydrophilic region, a region rich in serine, alanine, and proline/hydroxyproline, and a hydrophobic C-terminus. It is postulated to contain a GPI (glycosylphosphatidylinositol) anchor site. If the protein is cleaved at the putative GPI anchor site, as has been observed in other classical AGPs, all but the Ser-Ala-Pro/Hyp-rich domain may be missing from the mature protein. Xylem-specific AGPs are hypothesized to be involved in xylem development. Received: 29 July 1999 / Accepted: 19 August 1999 |
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Keywords: | : Arabinogalactan-protein – Pinus (AGP) – Xylem |
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