A reversibly glycosylated polypeptide (RGP1) possibly involved in plant cell wall synthesis: purification, gene cloning, and trans-Golgi localization.

@article{Dhugga1997ARG,
  title={A reversibly glycosylated polypeptide (RGP1) possibly involved in plant cell wall synthesis: purification, gene cloning, and trans-Golgi localization.},
  author={Kanwarpal S Dhugga and Soni Tiwari and Peter Martin Ray},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1997},
  volume={94 14},
  pages={
          7679-84
        }
}
  • K. Dhugga, S. Tiwari, P. Ray
  • Published 8 July 1997
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
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… 
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A multigenic family of self-glycosylating proteins named reversibly glycosylated polypeptides, designated as RGPs, have been usually associated with carbohydrate metabolism, although they are an
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