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Titolo:
DIFFUSION-CONTROLLED DNA RECOGNITION BY AN UNFOLDED, MONOMERIC BZIP TRANSCRIPTION FACTOR
Autore:
BERGER C; PIUBELLI L; HADITSCH U; BOSSHARD HR;
Indirizzi:
UNIV ZURICH,INST BIOCHEM,WINTERTHURERSTR 190 CH-8057 ZURICH SWITZERLAND UNIV ZURICH,INST BIOCHEM CH-8057 ZURICH SWITZERLAND
Titolo Testata:
FEBS letters
fascicolo: 1, volume: 425, anno: 1998,
pagine: 14 - 18
SICI:
0014-5793(1998)425:1<14:DDRBAU>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
LEUCINE-ZIPPER PROTEINS; BINDING DOMAINS; DIMERIZATION; COMPLEX; DIMER; GRIP; SITE; SPECIFICITY; MECHANISM; PEPTIDE;
Keywords:
PROTEIN-DNA RECOGNITION; KINETIC MECHANISM; TRANSCRIPTION FACTOR GCN4; MONOMER-DIMER EQUILIBRIUM; FLUORESCENCE-LABELED DNA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
32
Recensione:
Indirizzi per estratti:
Citazione:
C. Berger et al., "DIFFUSION-CONTROLLED DNA RECOGNITION BY AN UNFOLDED, MONOMERIC BZIP TRANSCRIPTION FACTOR", FEBS letters, 425(1), 1998, pp. 14-18

Abstract

Basic leucine zipper (bZIP) transcription factors are diners that recognize mainly palindromic DNA sites. It has been assumed that bZIP factors have to form a dimer in order to bind to their target DNA, We find that DNA binding of both monomeric and dimeric bZIP transcription factor GCN4 is diffusion-limited and that, therefore, the rate of dimerization of the bZIP domain does not affect the rate of DNA recognition and GCN4 need not dimerize in order to bind to its specific DNA site, The results have implications for the mechanism by which bZIP transcription factors find their target sites for transcriptional regulation, (C) 1998 Federation of European Biochemical Societies.

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Documento generato il 27/09/20 alle ore 12:36:22