Purification and cloning of an arabinogalactan-protein from xylem of loblolly pine. Academic Article uri icon


  • 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.

published proceedings

  • Planta

altmetric score

  • 6

author list (cited authors)

  • Loopstra, C. A., Puryear, J. D., & No, E. G.

citation count

  • 39

complete list of authors

  • Loopstra, CA||Puryear, JD||No, EG

publication date

  • January 2000