Cloning and Characterization of AtRGP11 : A Reversibly Autoglycosylated Arabidopsis Protein Implicated in Cell Wall Biosynthesis
| Autor: | Delgado, Ivan J., Wang, Zhaohong, de Rocher, Amy, Keegstra, Kenneth, Raikhel, Natasha V. |
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| Jazyk: | angličtina |
| Rok vydání: | 1998 |
| Předmět: |
DNA
Complementary Glycosylation Sequence Homology Amino Acid Arabidopsis Proteins Molecular Sequence Data Arabidopsis food and beverages Membrane Proteins carbohydrates (lipids) Solubility Cell Wall Polysaccharides Escherichia coli Amino Acid Sequence RNA Messenger Cloning Molecular Research Article Glycoproteins Plant Proteins |
| Popis: | A reversibly glycosylated polypeptide from pea (Pisum sativum) is thought to have a role in the biosynthesis of hemicellulosic polysaccharides. We have investigated this hypothesis by isolating a cDNA clone encoding a homolog of Arabidopsis thaliana, Reversibly Glycosylated Polypeptide-1 (AtRGP1), and preparing antibodies against the protein encoded by this gene. Polyclonal antibodies detect homologs in both dicot and monocot species. The patterns of expression and intracellular localization of the protein were examined. AtRGP1 protein and RNA concentration are highest in roots and suspension-cultured cells. Localization of the protein shows it to be mostly soluble but also peripherally associated with membranes. We confirmed that AtRGP1 produced in Escherichia coli could be reversibly glycosylated using UDP-glucose and UDP-galactose as substrates. Possible sites for UDP-sugar binding and glycosylation are discussed. Our results are consistent with a role for this reversibly glycosylated polypeptide in cell wall biosynthesis, although its precise role is still unknown. |
| Databáze: | OpenAIRE |
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