Abstract
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.
MeSH Terms
Amino Acid Sequence
Arabidopsis/genetics,metabolism
Arabidopsis Proteins
Cell Wall/metabolism
Cloning, Molecular
DNA, Complementary
Escherichia coli/genetics
Glycoproteins/genetics,metabolism
Glycosylation
Membrane Proteins/genetics,metabolism
Molecular Sequence Data
Plant Proteins/genetics,metabolism
Polysaccharides/biosynthesis
RNA, Messenger/genetics,metabolism
Sequence Homology, Amino Acid
Solubility
Chemicals
Arabidopsis Proteins
DNA, Complementary
Glycoproteins
Membrane Proteins
Plant Proteins
Polysaccharides
RGP1 protein, Arabidopsis
RNA, Messenger
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Delgado I J
Department of Energy Plant Research Laboratory, Michigan State University, East Lansing 48824-1312, USA.
Wang Z
de Rocher A
Keegstra K
Raikhel N V
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