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Titolo:
CHARACTERIZATION OF A PROTEIN THAT BINDS TO AT-RICH DNA IN A SEED NUCLEAR EXTRACT OF WINGED BEAN [PSOPHOCARPUS-TETRAGONOLOBUS (L.) DC. CV ISHIGAKI-4]
Autore:
HABU Y; FUKASAWA K; FURUYA S; MATSUMOTO D; OHNO T;
Indirizzi:
NATL INST BASIC BIOL OKAZAKI AICHI 444 JAPAN HOKKAIDO UNIV,DEPT APPL BIOSCI SAPPORO HOKKAIDO 060 JAPAN
Titolo Testata:
Journal of plant physiology
fascicolo: 1, volume: 152, anno: 1998,
pagine: 10 - 16
SICI:
0176-1617(1998)152:1<10:COAPTB>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
CHYMOTRYPSIN INHIBITOR GENE; GROUP CHROMOSOMAL-PROTEINS; HMG-BOX PROTEINS; FACTORS INTERACT; UPSTREAM REGION; PROMOTER; SEQUENCE; TRANSCRIPTION; ELEMENTS; EXPRESSION;
Keywords:
PSOPHOCARPUS TETRAGONOLOBUS (L.) DC. CV ISHIGAKI-4; AT-RICH SEQUENCES; DNA-BINDING PROTEINS; HMG-LIKE PROTEINS; KUNITZ PROTEINASE INHIBITOR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
30
Recensione:
Indirizzi per estratti:
Citazione:
Y. Habu et al., "CHARACTERIZATION OF A PROTEIN THAT BINDS TO AT-RICH DNA IN A SEED NUCLEAR EXTRACT OF WINGED BEAN [PSOPHOCARPUS-TETRAGONOLOBUS (L.) DC. CV ISHIGAKI-4]", Journal of plant physiology, 152(1), 1998, pp. 10-16

Abstract

The organ-specific and temporally regulated expression of the genes for Kunitz chymotrypsin inhibitor-3 in winged bean is known to be governed by its 5' flanking region. Two nuclear factors that bind to AT-rich sequences in this region were detected in gel retardation assays. The binding activity of one of these factors, band 1-forming factor, wasinhibited by phosphorylation, as is the AT-binding protein ATBP-1 of tobacco, which functions as an activator of transcription. In addition, the binding of band 1-forming factor was reduced in the presence of a low concentration of the minor groove-binding dye, Hoechst 33258, suggesting that band 1-forming factor recognizes the minor groove of-theprobe, as does ATBP-1. The binding of another factor, band 3-forming factor, was also reduced by Hoechst 33258, but the binding activity ofthis factor was not: affected by phosphorylation. During partial purification by gel-filtration and affinity chromatography, the binding activity of band 3-forming Factor was cofractionated with a 75-ku (kDa) DNA-binding protein. These results indicate that band 3-forming factoris a new DNA-binding factor that recognizes the minor groove of AT-rich DNA.

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Documento generato il 01/12/20 alle ore 07:40:43