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Titolo:
PURIFICATION AND CHARACTERIZATION OF A SOLUBLE SALICYLIC ACID-BINDINGPROTEIN FROM TOBACCO
Autore:
CHEN ZX; RICIGLIANO JW; KLESSIG DF;
Indirizzi:
RUTGERS UNIV,WAKSMAN INST PISCATAWAY NJ 08855 RUTGERS UNIV,WAKSMAN INST PISCATAWAY NJ 08855
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 20, volume: 90, anno: 1993,
pagine: 9533 - 9537
SICI:
0027-8424(1993)90:20<9533:PACOAS>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
PATHOGENESIS-RELATED PROTEINS; RESISTANCE RESPONSE; PLANT-DISEASE; MOSAIC-VIRUS; INDUCTION; CUCUMBER; ASPIRIN; SIGNAL;
Keywords:
MONOCLONAL ANTIBODY; PATHOGENESIS-RELATED PROTEINS; PLANT DEFENSE MECHANISM; PLANT SIGNAL TRANSDUCTION; SYSTEMIC ACQUIRED RESISTANCE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
21
Recensione:
Indirizzi per estratti:
Citazione:
Z.X. Chen et al., "PURIFICATION AND CHARACTERIZATION OF A SOLUBLE SALICYLIC ACID-BINDINGPROTEIN FROM TOBACCO", Proceedings of the National Academy of Sciences of the United Statesof America, 90(20), 1993, pp. 9533-9537

Abstract

Previously, we identified a soluble salicylic acid (SA)-binding protein (SABP) in tobacco whose properties suggest that it may play a role in transmitting the SA signal during plant defense responses. This SA-binding activity has been purified 250-fold by conventional chromatography and was found to copurify with a 280-kDa protein. Monoclonal antibodies capable of immunoprecipitating the SA-binding activity also immunoprecipitated the 280-kDa protein, indicating that it was responsible for binding SA. These antibodies also recognized the 280-kDa proteinin immunoblots of the partially purified SABP fraction or the crude extract. However, when the crude extract was prepared in the presence of antioxidants, only a 57-kDa protein was recognized. Since the SABP has a native molecular mass of 240 kDa, it appears that the SABP is a complex which contains a 57-kDa subunit and perhaps one or more additional proteins which are covalently crosslinked in the absence of antioxidants. The ability of a variety of phenolic compounds to compete withSA for binding to the SABP was both qualitatively and quantitatively correlated with their biological activity in inducing defense-related genes. Moreover, the inducibility of the pathogenesis-related (PR)-1 genes by SA was proportional to the abundance of the SABP in different organs. These correlations are consistent with a role for the SABP in perceiving and transducing the SA signal in plant defense.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/03/20 alle ore 15:40:49