MOLECULAR-CLONING OF A GENE ENCODING AN ARABINOGALACTAN PROTEIN FROM PEAR (PYRUS-COMMUNIS) CELL-SUSPENSION CULTURE
- Author(s)
- CHEN, CG; PU, ZY; Moritz, RL; Simpson, RJ; Bacic, A; Clarke, AE; MAU, SL;
- Details
- Publication Year 1994-10-25,Volume 91,Issue #22,Page 10305-10309
- Journal Title
- PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Publication Type
- Journal Article
- Abstract
- Arabinogalactan proteins (AGPs) are proteoglycans containing a high proportion of carbohydrate (typically >90%) linked to a protein backbone rich in hydroxyproline (Hyp), Ala, Ser, and Thr. They are widely distributed in plants and may play a role in development. The structure of the carbohydrate of some AGPs is known in detail but information regarding the protein backbone is restricted to a few peptide sequences. Here we report isolation and partial amino acid sequencing of the protein backbone of an AGP, This AGP is a member of one of four major groups of AGPs isolated from the filtrate of pear cell suspension culture. A cDNA encoding this protein backbone (145 amino acids) was cloned; the deduced protein is rich in Hyp, Ala, Ser, and Thr, which together account for >75% of total residues. It has three domains, an N-terminal secretion signal, a central hydrophilic domain containing all of the Pro residues, and a hydrophobic C-terminal domain that is predicted to be a transmembrane helix. Approximately 93% of the Pro residues are hydroxylated and hence are potential sites for glycosylation.
- Publisher
- NATL ACAD SCIENCES
- Keywords
- PLASMA-MEMBRANE; DAUCUS-CAROTA; SEQUENCE; CHROMATOGRAPHY; PURIFICATION
- Publisher's Version
- https://doi.org/10.1073/pnas.91.22.10305
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 1994-10-25 12:00:00