DOI: 10.1111/j.1432-1033.1986.tb09803.x. The position of the oligosaccharide side‐chains of phytohemagglutinin and their accessibility to glycosidases determines their subsequent processing in the Golgi

The position of the oligosaccharide side‐chains of phytohemagglutinin and their accessibility to glycosidases determines their subsequent processing in the Golgi

10.1111/j.1432-1033.1986.tb09803.x

Crossref journal-article

Wiley

European Journal of Biochemistry (311)

Abstract

Phytohemagglutinin (PHA), the glycoprotein lectin of Phaseolus vulgaris has two types of asparagine‐linked oligosaccharides per polypeptide: a high‐mannose chain with the formula (Man)8–9(GlcNAc)2 on Asn12 and a modified chain with fewer mannose residues and additional fucose and xylose residues on Asn60. Glycosylation of PHA is a cotranslational process, which occurs in the endoplasmic reticulum, and newly synthesized PHA has two high‐mannose chains. Transport of PHA to the protein bodies via the Golgi complex is accompanied by the modification of one of the two high‐mannose chains. Why is only one chain modified, while the other remains in the high‐mannose configuration? By determining the effect of digestion with various glycosidases (α‐mannosidase, endo‐β‐N‐acetylglucosaminidase H and endo‐β‐N‐acetylglucosaminidase F) on native and denatured PHA we obtained evidence consistent with the interpretation that the accessibility of oligosaccharide chains to modifying enzymes is of major importance in determining whether a high‐mannose chain becomes modified or not. The high‐mannose chain of mature undenatured PHA is only partially accessible to glycosidases, while PHA obtained from the endoplasmic reticulum has one high‐mannose chain, which is readily accessible to α‐mannosidase and endoglycosidases H and F. We show that this readily accessible chain is in the same position on the polypeptide (Asn60) as the modified oligosaccharide on mature PHA. Thus, accessibility of the oligosaccharide side‐chains to processing enzymes in the Golgi determines whether a particular oligosaccharide side‐chain is processed or not.

Bibliography

FAYE, L., STURM, A., BOLLINI, R., VITALE, A., & CHRISPEELS, M. J. (1986). The position of the oligosaccharide sideâchains of phytohemagglutinin and their accessibility to glycosidases determines their subsequent processing in the Golgi. European Journal of Biochemistry, 158(3), 655â661. Portico.

Authors 5

Loic FAYE (first)
Arnd STURM (additional)
Roberto BOLLINI (additional)
Alessandro VITALE (additional)
Maarten J. CHRISPEELS (additional)

References 28 Referenced 54

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10.1111/j.1432-1033.1982.tb19760.x
10.1007/BF00402863
10.1111/j.1432-1033.1985.tb08737.x
{'key': 'e_1_2_3_10_2', 'first-page': '49', 'volume-title': 'Glycoconjugates, Proc. 8th Int. Symp.', 'author': 'Ikemaka T.', 'year': '1985'} / Glycoconjugates, Proc. 8th Int. Symp. by Ikemaka T. (1985)
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10.1016/S0021-9258(18)32962-4 / J. Biol. Chem. by Hsieh P. (1983)
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Dates

Type	When
Created	20 years, 5 months ago (March 3, 2005, 7:41 p.m.)
Deposited	1 year, 9 months ago (Nov. 23, 2023, 9:55 a.m.)
Indexed	3 weeks, 2 days ago (Aug. 5, 2025, 8:40 a.m.)
Issued	39 years ago (Aug. 1, 1986)
Published	39 years ago (Aug. 1, 1986)
Published Online	20 years, 5 months ago (March 3, 2005)
Published Print	39 years ago (Aug. 1, 1986)

Funders 0

None

BibTeX

@article{FAYE_1986, title={The position of the oligosaccharide side‐chains of phytohemagglutinin and their accessibility to glycosidases determines their subsequent processing in the Golgi}, volume={158}, ISSN={1432-1033}, url={http://dx.doi.org/10.1111/j.1432-1033.1986.tb09803.x}, DOI={10.1111/j.1432-1033.1986.tb09803.x}, number={3}, journal={European Journal of Biochemistry}, publisher={Wiley}, author={FAYE, Loic and STURM, Arnd and BOLLINI, Roberto and VITALE, Alessandro and CHRISPEELS, Maarten J.}, year={1986}, month=aug, pages={655–661} }

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