Abstract
We purified from pea (Pisum sativum) tissue an approximately 40 kDa reversibly glycosylated polypeptide (RGP1) that can be glycosylated by UDP-Glc, UDP-Xyl, or UDP-Gal, and isolated a cDNA encoding it, apparently derived from a single-copy gene (Rgp1). Its predicted translation product has 364 aminoacyl residues and molecular mass of 41.5 kDa. RGP1 appears to be a membrane-peripheral protein. Immunogold labeling localizes it specifically to trans-Golgi dictyosomal cisternae. Along with other evidence, this suggests that RGP1 is involved in synthesis of xyloglucan and possibly other hemicelluloses. Corn (Zea mays) contains a biochemically similar and structurally homologous RGP1, which has been thought (it now seems mistakenly) to function in starch synthesis. The expressed sequence database also reveals close homologs of pea Rgp1 in Arabidopsis and rice (Oryza sativa). Rice possesses, in addition, a distinct but homologous sequence (Rgp2). RGP1 provides a polypeptide marker for Golgi membranes that should be useful in plant membrane studies.
MeSH Terms
Amino Acid Sequence
Arabidopsis Proteins
Cell Wall/metabolism
Cloning, Molecular
Glycoproteins/genetics,isolation & purification
Golgi Apparatus/metabolism
Molecular Sequence Data
Peas/genetics
Plant Proteins/genetics,isolation & purification
Sequence Alignment
Chemicals
Arabidopsis Proteins
Glycoproteins
Plant Proteins
RGP1 protein, Arabidopsis
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Dhugga K S
Department of Biological Sciences, Stanford University, Stanford, CA 94305, USA.
Tiwari S C
Ray P M
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