Plant Physiol. Drug Metab Dispos
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Plant Physiology 84:1301-1308 (1987)
© 1987 American Society of Plant Biologists

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Johnson, K. D.
Right arrow Articles by Chrispeels, M. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Johnson, K. D.
Right arrow Articles by Chrispeels, M. J.
Agricola
Right arrow Articles by Johnson, K. D.
Right arrow Articles by Chrispeels, M. J.
Cellular and Structural Biology

Substrate Specificities of N-Acetylglucosaminyl-, Fucosyl-, and Xylosyltransferases that Modify Glycoproteins in the Golgi Apparatus of Bean Cotyledons 1

Kenneth D. Johnson and Maarten J. Chrispeels

Department of Biology, San Diego State University, San Diego, California 92182, Department of Biology, University of California, San Diego, La Jolla, California 92093

As part of their posttranslational maturation process, newly synthesized glycoproteins that contain N-linked oligosaccharide side chains pass through the Golgi apparatus, where some of their oligosaccharides become modified by carbohydrate processing reactions. In this paper, we report the presence of Golgi-localized enzymes in plant cells (Phaseolus vulgaris cotyledons) that transfer GlcNAc, fucosyl, and xylosyl residues to the oligosaccharide side chains of glycoproteins. All three enzyme activities are involved in the transformation of high mannose side chains into complex glycans. As judged by acceptor specificity studies, at least two GlcNAc residues can be added to the nonreducing side of high mannose oligosaccharides, which have been trimmed by {alpha}-mannosidase(s). A Man5(GlcNAc)2-peptide serves as the acceptor for the first GlcNAc added. The second GlcNAc can be added only after the prior removal of two additional mannose residues, ultimately yielding (GlcNAc)2Man3(GlcNAc)2-peptide. Fucosyltransferase can transfer fucose to GlcNAcMan5(GlcNAc)2Asn, GlcNAcMan3(GlcNAc)2Asn, and (GlcNAc)2Man3(GlcNAc)2Asn; xylosyltransferase exhibits significant activity toward the latter two substrates only. These results suggest an overlapping sequence of oligosaccharide modification in the Golgi apparatus that, in regard to GlcNAc and fucose additions, is analogous to pathways of oligosaccharide processing reported for animal cells. To our knowledge, this is the first report characterizing a xylosyltransferase involved in N-linked oligosaccharide modification, an activity that is apparently absent in most animal cells.

1 Supported in part by a grant to K. D. J. from the San Diego State University Foundation, and by grants to M. J. C. from the United States Department of Energy and the National Science Foundation (Metabolic Biology).




This article has been cited by other articles:


Home page
 Proc. Natl. Acad. Sci. USAHome page
J. S. Kang, J. Frank, C. H. Kang, H. Kajiura, M. Vikram, A. Ueda, S. Kim, J. D. Bahk, B. Triplett, K. Fujiyama, et al.
Salt tolerance of Arabidopsis thaliana requires maturation of N-glycosylated proteins in the Golgi apparatus
PNAS, April 15, 2008; 105(15): 5933 - 5938.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
M. Crispin, D. J. Harvey, V. T. Chang, C. Yu, A. R. Aricescu, E. Y. Jones, S. J. Davis, R. A. Dwek, and P. M. Rudd
Inhibition of hybrid- and complex-type glycosylation reveals the presence of the GlcNAc transferase I-independent fucosylation pathway
Glycobiology, August 1, 2006; 16(8): 748 - 756.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
H. Bakker, G. J. A. Rouwendal, A. S. Karnoup, D. E. A. Florack, G. M. Stoopen, J. P. F. G. Helsper, R. van Ree, I. van Die, and D. Bosch
An antibody produced in tobacco expressing a hybrid beta-1,4-galactosyltransferase is essentially devoid of plant carbohydrate epitopes
PNAS, May 16, 2006; 103(20): 7577 - 7582.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
H. Bakker, M. Bardor, J. W. Molthoff, V. Gomord, I. Elbers, L. H. Stevens, W. Jordi, A. Lommen, L. Faye, P. Lerouge, et al.
Galactose-extended glycans of antibodies produced by transgenic plants
PNAS, February 27, 2001; 98(5): 2899 - 2904.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
S. Pagny, M. Cabanes-Macheteau, J. W. Gillikin, N. Leborgne-Castel, P. Lerouge, R. S. Boston, L. Faye, and V. Gomord
Protein Recycling from the Golgi Apparatus to the Endoplasmic Reticulum in Plants and Its Minor Contribution to Calreticulin Retention
PLANT CELL, May 1, 2000; 12(5): 739 - 756.
[Abstract] [Full Text]

Home page
 Proc. Natl. Acad. Sci. USAHome page
N. Q. Palacpac, S. Yoshida, H. Sakai, Y. Kimura, K. Fujiyama, T. Yoshida, and T. Seki
Stable expression of human beta 1,4-galactosyltransferase in plant cells modifies N-linked glycosylation patterns
PNAS, April 13, 1999; 96(8): 4692 - 4697.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1987 by the American Society of Plant Biologists