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Titolo:
A NOVEL PATHOGEN-INDUCIBLE AND WOUND-INDUCIBLE TOBACCO (NICOTIANA-TABACUM) PROTEIN WITH ANTIFUNGAL ACTIVITY
Autore:
PONSTEIN AS; BRESVLOEMANS SA; SELABUURLAGE MB; VANDENELZEN PJM; MELCHERS LS; CORNELISSEN BJC;
Indirizzi:
MOGEN INT NV 2333 CB LEIDEN NETHERLANDS
Titolo Testata:
Plant physiology
fascicolo: 1, volume: 104, anno: 1994,
pagine: 109 - 118
SICI:
0032-0889(1994)104:1<109:ANPAWT>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
TREE HEVEA-BRASILIENSIS; SODIUM DODECYL-SULFATE; PLANT DEFENSE; ACQUIRED-RESISTANCE; POLYACRYLAMIDE GELS; BIOLOGICAL FUNCTION; VIRUS-INFECTION; MESSENGER-RNA; FUNGAL GROWTH; RICH DOMAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
58
Recensione:
Indirizzi per estratti:
Citazione:
A.S. Ponstein et al., "A NOVEL PATHOGEN-INDUCIBLE AND WOUND-INDUCIBLE TOBACCO (NICOTIANA-TABACUM) PROTEIN WITH ANTIFUNGAL ACTIVITY", Plant physiology, 104(1), 1994, pp. 109-118

Abstract

A novel pathogen- and wound-inducible antifungal protein of 20 kD waspurified from tobacco (Nicotiana tabacum) Samsun NN leaves inoculatedwith tobacco mosaic virus (TMV). The protein, designated CBP20, was purified by chitin-affinity chromatography and gel filtration. In vitroassays demonstrated that CBP20 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 CBP20 acts synergistically with a tobacco class I chitinase against F. solani and with a tobacco class 1 beta-1,3-glucanase against F. solani and Alternaria radicina. Analysis of the protein and corresponding cDNAs revealed that CBP20 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, WIN1: and WIN2, and several plant lectins. The C-terminaI domain of CBP20 showed high identity with tobacco pathogenesis-related (PR) proteins, PR-4a and PR-4b, tomato PR-P2, and potato WIN1 and WIN2. CBP20 is synthesized as a preproprotein, which isprocessed 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 CBP20 and its induction upon TMV infection and wounding indicate that CBP20 is the first class I PR-4 type protein purified.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 04:44:03