A nove1 pathogen-and wound-inducible antifungal protein of 20 kD was purified from tobacco (Nicotiana tabacum) Samsun NN leaves inoculated with tobacco mosaic virus (TMV). The protein, designated CBPZO, was purified by chitin-affinity chromatography and gel filtration. In vitro assays demonstrated that CBPZO exhibits antifungal activity toward Trichoderma viride and Fusarium solani by causing lysis of the germ tubes and/or growth inhibition. In addition it was shown that CBPZO acts synergistically with a tobacco class I chitinase against F. solani and with a tobacco class I &1,3-glucanase against F. solani and Alternaria radicina. Analysis of the protein and corresponding cDNAs revealed that CBPZO contains an N-terminal chitin-binding domain that is present also in the class I chitinases of tobacco, the putative wound-induced (WIN) proteins of potato, W l N l and WINZ, and severa1 plant lectins. The C-terminal domain of CBPZO showed high identity with tobacco pathogenesis-related (PR) proteins, PR-4a and PR-4b, tomato PR-P2, and potato W l N l and WIN2. CBPZO is synthesized as a preproprotein, which is processed into the mature protein by the removal of an N-terminal signal peptide and a C-terminal propeptide, most likely involved in the vacuolar targeting of the protein. The intracellular localization of CBPZO and its induction upon TMV infection and wounding indicate that CBPZO is the first class I PR-4 type protein purified.
A new class of tobacco chitinases homologous to bacterial exo-chitinases displays antifungal activity Melchers, L.S.; Apotheker-de Groot, M.; van der Knaap, J.A.; Ponstein, A.P.; Sela-Buurlage, M.B.; Bol, J.F.; Cornelissen, B.J.C.; van den Elzen, P.J.M.; Linthorst, H.J.M. Published in:Plant Journal Link to publication Citation for published version (APA):Melchers, L. S., Apotheker-de Groot, M., van der Knaap, J. A., Ponstein, A. P., Sela-Buurlage, M. B., Bol, J. F., ... Linthorst, H. J. M. (1994). A new class of tobacco chitinases homologous to bacterial exo-chitinases displays antifungal activity. Plant Journal, 5, 469-480. General rightsIt is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), other than for strictly personal, individual use, unless the work is under an open content license (like Creative Commons). Disclaimer/Complaints regulationsIf you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: http://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. Download date: 12 May 2018The Plant Joumal (1994) Two related chitinsse class V proteins of 41 and 43 kDa were purified from Samsun NN tobacco leaves inoculated with tobacco mosaic virus. The proteins were purified by Chelating Suparose chromatography and gel filtration. In vitro assays demonstrated that class V chitinaeas have endo-chitinase activity and exhibit antifungal activity toward Trichoderma viride and Alternaria radicina. In addition, it was shown that class V chitlnase acts synergistically with tobacco class I 1~-l,3-glucanase agalnat Fusarlum solani germlings.
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