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Titolo:
Role of conserved residues of the WRKY domain in the DNA-binding of tobacco WRKY family proteins
Autore:
Maeo, K; Hayashi, S; Kojima-Suzuki, H; Morikami, A; Nakamura, K;
Indirizzi:
Nagoya Univ, Grad Sch Bioagr Sci, Dept Cellular Mech & Funct, Lab Biochem,Chikusa Ku, Nagoya, Aichi 4648601, Japan Nagoya Univ Nagoya Aichi Japan 4648601 a Ku, Nagoya, Aichi 4648601, Japan
Titolo Testata:
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
fascicolo: 11, volume: 65, anno: 2001,
pagine: 2428 - 2436
SICI:
0916-8451(200111)65:11<2428:ROCROT>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
NO APICAL MERISTEM; TRANSCRIPTION FACTORS; SWEET-POTATO; INDUCIBLE EXPRESSION; RESPONSE ELEMENTS; SALICYLIC-ACID; BETA-AMYLASE; GENES; ARABIDOPSIS; ACTIVATOR;
Keywords:
transcription factor; DNA-binding domain; WRKY domain; tobacco; plant-specific zinc finger;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
25
Recensione:
Indirizzi per estratti:
Indirizzo: Maeo, K Nagoya Univ, Grad Sch Bioagr Sci, Dept Cellular Mech & Funct, Lab Biochem,Chikusa Ku, Nagoya, Aichi 4648601, Japan Nagoya Univ Nagoya Aichi Japan 4648601 goya, Aichi 4648601, Japan
Citazione:
K. Maeo et al., "Role of conserved residues of the WRKY domain in the DNA-binding of tobacco WRKY family proteins", BIOS BIOT B, 65(11), 2001, pp. 2428-2436

Abstract

Four cDNA clones of tobacco that could code for pol peptides with two WRKYdomains were isolated. Among four NtWRKYs and other WRKY family proteins, sequence similarity was basically limited to the two WRKY domains. Glutathione S-transferase fusion proteins with the C-terminal WRKY domain of four NtWRKYs bound specifically to the W-box (TTGACC), and the N-terminal WRKY domain showed weaker binding activity with the W-box compared to the C-terminal domain. The DNA-binding activity of the WRKY domain was abolished by o-phenanthroline and this inhibition was recovered specifically by Zn2-. Substitution of the conserved cysteine and histidine residues of the plant-specific C2H2-type zinc finger-like motif in the WRKY domain abolished the DNA binding. In addition, mutations in the invariable WRKYGQK sequence at the N-terminal side of the zinc finger-like motif also significantly reduced the DNA-binding activity, suggesting that these residues are required for proper folding of the DNA-binding zinc finger.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 20:21:06