Abstract
Proteins secreted by suspension cultured tobacco cells were analysed. Nineteen clearly separated polypeptide bands (designated SN1 to SN19) between 6 and 100 kDa were reproducibly found after SDS-PAGE. Brefeldin A (BFA) strongly inhibits protein secretion including secretion of apoplastic peroxidase which was used as an indicator for BFA effects on glycosylated proteins passing through the endomembrane system. The labelling of secreted proteins is strongly decreased by short-term (20 µM BFA, up to 4 h) as well as by long-term (2 µM BFA, up to 3 d) incubation with the drug whereas neither the uptake into cells nor the incorporation of 35S-methionine into cellular proteins was affected by the drug. In contrast to the majority of secretory proteins the polypeptides SN1, SN8, SN9 and SN11 were not significantly affected by the drug. The differential BFA effects can not be related to proteolysis in the culture medium. N-terminal sequences of SN9 and SN11 are similar to a region within chitin binding domains of class I chitinases of tobacco.
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© 1995 Springer Science+Business Media Dordrecht
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Kunze, I., Horstmann, C., Manteuffel, R., Kunze, G., Müntz, K. (1995). Brefeldin A differentially affects protein secretion from suspension cultured tobacco cells (Nico-tiana tabacum L.). In: Terzi, M., Cella, R., Falavigna, A. (eds) Current Issues in Plant Molecular and Cellular Biology. Current Plant Science and Biotechnology in Agriculture, vol 22. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-0307-7_89
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DOI: https://doi.org/10.1007/978-94-011-0307-7_89
Publisher Name: Springer, Dordrecht
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