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Titolo:
A chimera of Urtica dioica agglutinin and tobacco chitinase displays both agglutination and chitinase activity
Autore:
Does, MP; Cornelissen, BJC;
Indirizzi:
Bioctr Amsterdam, Inst Mol Cell Biol, Sect Plant Biol, NL-1098 SM Amsterdam, Netherlands Bioctr Amsterdam Amsterdam Netherlands NL-1098 SM Amsterdam, Netherlands
Titolo Testata:
PLANT SCIENCE
fascicolo: 2, volume: 148, anno: 1999,
pagine: 121 - 129
SICI:
0168-9452(19991029)148:2<121:ACOUDA>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
HYDROXYPROLINE-CONTAINING PROTEINS; CYSTEINE-RICH DOMAIN; ANTIFUNGAL ACTIVITY; BINDING; LECTIN; GENES; EXPRESSION; RHIZOMES; SEQUENCE; CLEAVAGE;
Keywords:
fusion protein; stinging nettle lectin; tobacco chitinase I; agglutination activity; chitinase activity;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: Does, MP Bioctr Amsterdam, Inst Mol Cell Biol, Sect Plant Biol, Kruislaan 318, NL-1098 SM Amsterdam, Netherlands Bioctr Amsterdam Kruislaan 318 Amsterdam Netherlands NL-1098 SM
Citazione:
M.P. Does e B.J.C. Cornelissen, "A chimera of Urtica dioica agglutinin and tobacco chitinase displays both agglutination and chitinase activity", PLANT SCI, 148(2), 1999, pp. 121-129

Abstract

To obtain a protein with agglutination activity as well as chitinase activity, a fusion protein was designed in which Urtica dioica agglutinin (UDA)-isolectin I and the catalytic domain of tobacco (Nicotiana tabacum cv. Samsun NN) chitinase I were assembled. A, construct was made containing sequences encoding the signal peptide and the isolectin sequence of the precursor to UDA-isolectin I, followed by the linker and the catalytic domain of tobacco chitinase I. Due to the introduction of a stopcodon, the precursor to this chimera lacked the seven carboxyl-terminal amino acids necessary for vacuolar targeting of tobacco chitinase I. The construct was expressed in transgenic tobacco (Nicotiana tabacum cv. Samsun NN) under control of the cauliflower mosaic virus 35S promoter. Analysis of transgenic plants showed that the fusion protein UDA-Chi is targeted extracellularly. Both crude leaf extracts of transgenic tobacco and purified fusion protein showed agglutination activity on trypsin-treated rabbit erythrocytes. The molar agglutination activity of the UDA-Chi chimera was shown to be similar to that of matureUDA. The chimera has chitinase activity that differs from that of tobacco chitinase I. (C) 1999 Published by Elsevier Science Ireland Ltd. All rightsreserved.

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Documento generato il 04/07/20 alle ore 15:02:41