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Titolo:
THE N-TERMINAL CYSTEINE-RICH DOMAIN OF TOBACCO CLASS-I CHITINASE IS ESSENTIAL FOR CHITIN-BINDING BUT NOT FOR CATALYTIC OR ANTIFUNGAL ACTIVITY
Autore:
ISELI B; BOLLER T; NEUHAUS JM;
Indirizzi:
UNIV BASEL,INST BOT,HEBELSTR 1 CH-4056 BASEL SWITZERLAND UNIV BASEL,INST BOT,HEBELSTR 1 CH-4056 BASEL SWITZERLAND
Titolo Testata:
Plant physiology
fascicolo: 1, volume: 103, anno: 1993,
pagine: 221 - 226
SICI:
0032-0889(1993)103:1<221:TNCDOT>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
PATHOGENESIS-RELATED PROTEINS; TREE HEVEA-BRASILIENSIS; TRANSGENIC PLANTS; FUNGAL GROWTH; LECTIN; GENE; AGGLUTININ; ETHYLENE; SEQUENCE; WHEAT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
30
Recensione:
Indirizzi per estratti:
Citazione:
B. Iseli et al., "THE N-TERMINAL CYSTEINE-RICH DOMAIN OF TOBACCO CLASS-I CHITINASE IS ESSENTIAL FOR CHITIN-BINDING BUT NOT FOR CATALYTIC OR ANTIFUNGAL ACTIVITY", Plant physiology, 103(1), 1993, pp. 221-226

Abstract

The vacuolar chitinases of class I possess an N-terminal cysteine-rich domain homologous to hevein and chitin-binding lectins such as wheatgerm agglutinin and Urtica dioica lectin. To investigate the significance of this domain for the biochemical and functional characteristicsof chitinase, chimeric genes encoding the basic chitinase A of tobacco (Nicotiana tabacum) with and without this domain were constructed and constitutively expressed in transgenic Nicotiana sylvestris. The chitinases were subsequently isolated and purified to homogeneity from the transgenic plants. Chromatography on colloidal chitin revealed that only the form with the N-terminal domain, and not the one without it, had chitin-binding properties, demonstrating directly that the domain is a chitin-binding domain (CBD). Under standard assay conditions withradioactive colloidal chitin, both forms of chitinase had approximately the same catalytic activity. However, kinetic analysis demonstratedthat the enzyme without CBD had a considerably lower apparent affinity for its substrate. The pH and temperature optima of the two chitinases were similar, but the form with the CBD had an approximately 3-foldhigher activation energy and retained a higher activity at low pH values. Both chitinases were capable of inhibiting growth of Trichoderma viride, although the form with the CBD was about three times more effective than the one without it. Thus, the CBD is not necessary for catalytic or antifungal activity of chitinase.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 04:24:24