Intracellular transport and processing of a tobacco vacuolar β-1,3-glucanase View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1992-11

AUTHORS

Liliane Sticher, Ursula Hinz, Alain D. Meyer, Frederick Meins

ABSTRACT

The class I β-1,3-glucanases are basic, vacuolar enzymes implicated in the defense of plants against pathogen infection. The tobacco (Nicotiana tabacum L.) enzyme is synthesized as a preproprotein with an N-terminal signal peptide for targeting to the lumen of the endoplasmic reticulum and an N-glycosylated C-terminal extension which is lost during protein maturation. The transport and processing of β-1,3-glucanase in cellsuspension cultures of the tobacco cultivar Havana 425 was investigated by pulse-chase labelling and cell fractionation. We verified that mature β-1,3-glucanase is localized in the vacuole of the suspension-cultured cells. Comparison of the time course of processing in homogenates, the soluble fraction, and membrane fractions indicates that proglucanase is transported from the endoplasmic reticulum via the Golgi compartment to the vacuole. Processing to the mature form occurs in the vacuole. Treatment of cells with tunicamycin, which inhibits N-glycosylation, and digestion of the 35S-labelled processing intermediates with endoglycosidase H indicate that β-1,3-glucanase has a single N-glycan attached to the C-terminal extension. Glycosylation is not required for proteolytic processing or correct targeting to the vacuole. More... »

PAGES

559-565

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00197049

DOI

http://dx.doi.org/10.1007/bf00197049

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1030147657

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/24178389


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