Abstract
The transport and accumulation of phytohemagglutinin in developing bean (Phaseolus vulgaris L.) cotyledons is accompanied by the transient presence of N-acetylglucosamine (GlcNAc) residues on the oligosaccharide sidechains of this glycoprotein. These peripheral GlcNAc residues can be distinguished from those in the chitobiose portion of the oligosaccharide sidechains by their sensitivity to removal by the exoglycosidase β-N-acetylglucosaminidase. GlcNAc residues sensitive to removal by β-N-acetylglucosaminidase are present not only on phytohemagglutinin, but also on other newly synthesized proteins. The enzyme UDPGlcNAc:glycoprotein GlcNAc-transferase which transfers GlcNAc residues to glycoproteins was first described by Davies and Delmer (Plant Physiol 1981 68: 284-291). The data presented here show that this enzyme is associated with the Golgi complex of developing cotyledons.
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- Bonner W. M., Laskey R. A. A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels. Eur J Biochem. 1974 Jul 1;46(1):83–88. doi: 10.1111/j.1432-1033.1974.tb03599.x. [DOI] [PubMed] [Google Scholar]
- Davies H. M., Delmer D. P. Two Kinds of Protein Glycosylation in a Cell-Free Preparation from Developing Cotyledons of Phaseolus vulgaris. Plant Physiol. 1981 Aug;68(2):284–291. doi: 10.1104/pp.68.2.284. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Felsted R. L., Leavitt R. D., Bachur N. R. Purification of the phytohemagglutinin family of proteins from red kidney beans (Phaseolus vulgaris) by affinity chromatography. Biochim Biophys Acta. 1975 Sep 9;405(1):72–81. doi: 10.1016/0005-2795(75)90316-5. [DOI] [PubMed] [Google Scholar]
- Gardiner M., Chrispeels M. J. Involvement of the Golgi Apparatus in the Synthesis and Secretion of Hydroxyproline-rich Cell Wall Glycoproteins. Plant Physiol. 1975 Mar;55(3):536–541. doi: 10.1104/pp.55.3.536. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gleeson P. A., Schachter H. Control of glycoprotein synthesis. J Biol Chem. 1983 May 25;258(10):6162–6173. [PubMed] [Google Scholar]
- Johnston I. R., McGuire E. J., Roseman S. Sialic acids. XVII. A uridine diphosphate N-acetylglucosamine:glycoprotein N-acetylglucosaminyltransferase from goat colostrum. J Biol Chem. 1973 Nov 10;248(21):7281–7288. [PubMed] [Google Scholar]
- Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
- Nagahashi J., Browder S. K., Beevers L. Glycosylation of pea cotyledon membranes. Plant Physiol. 1980 Apr;65(4):648–657. doi: 10.1104/pp.65.4.648. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Spencer D., Higgins T. J., Button S. C., Davey R. A. Pulse-labeling Studies on Protein Synthesis in Developing Pea Seeds and Evidence of a Precursor Form of Legumin Small Subunit. Plant Physiol. 1980 Sep;66(3):510–515. doi: 10.1104/pp.66.3.510. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Van Der Wilden W., Chrispeels M. J. Characterization of the Isozymes of alpha-Mannosidase Located in the Cell Wall, Protein Bodies, and Endoplasmic Reticulum of Phaseolus vulgaris Cotyledons. Plant Physiol. 1983 Jan;71(1):82–87. doi: 10.1104/pp.71.1.82. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Vitale A., Chrispeels M. J. Transient N-acetylglucosamine in the biosynthesis of phytohemagglutinin: attachment in the Golgi apparatus and removal in protein bodies. J Cell Biol. 1984 Jul;99(1 Pt 1):133–140. doi: 10.1083/jcb.99.1.133. [DOI] [PMC free article] [PubMed] [Google Scholar]