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Titolo:
Increased nuclear factor 1 binding to its nucleosomal site mediated by sequence-dependent DNA structure
Autore:
Blomquist, P; Belikov, S; Wrange, O;
Indirizzi:
Karolinska77nst, Med Nobel Inst, Dept Cell & Mol Biol, Mol Genet Lab, S-171 Karolinska Inst Stockholm Sweden S-17177 Mol Biol, Mol Genet Lab, S-171 Russian Acad Sci, WA Engelhardt Inst Mol Biol, Moscow 117984, Russia Russian Acad Sci Moscow Russia 117984 st Mol Biol, Moscow 117984, Russia
Titolo Testata:
NUCLEIC ACIDS RESEARCH
fascicolo: 2, volume: 27, anno: 1999,
pagine: 517 - 525
SICI:
0305-1048(19990115)27:2<517:INF1BT>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
TUMOR VIRUS PROMOTER; TRANSCRIPTION FACTOR ACCESS; FACILITATED BINDING; MMTV PROMOTER; FACTOR-I; POSITIONED NUCLEOSOMES; TRANSLATIONAL POSITION; CRYSTAL-STRUCTURE; REPLICATION; RECEPTOR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
45
Recensione:
Indirizzi per estratti:
Indirizzo: Wrange, O Karolinska77nst, Med Nobel Inst, Dept Cell & Mol Biol, Mol GenetLab, S-171 Karolinska Inst Stockholm Sweden S-17177 Mol Genet Lab, S-171
Citazione:
P. Blomquist et al., "Increased nuclear factor 1 binding to its nucleosomal site mediated by sequence-dependent DNA structure", NUCL ACID R, 27(2), 1999, pp. 517-525

Abstract

The organization of DNA into chromatin is important in the regulation of transcription, by influencing the access of transcription factors to their DNA binding sites. Nuclear factor 1 (NF-1) is a transcription factor which binds to DNA constitutively and which interacts with its cognate DNA site with high affinity. However, this affinity is drastically reduced, similar to100- to 300-fold, when the binding site is organized into a nucleosome. Here we demonstrate that the introduction of stretches of adenines of length 5 nt (A-tracts) on both sides of the NF-1 binding site has a distinct effect on NF-1 binding to a nucleosomal, but not to a free, NF-1 binding site, The position of the A-tracts, relative to the rotational phase of a synthetic DNA bending sequence, the TG-motif, decides whether the NF-1 affinity increases or decreases. The NF-1 binding affinity is seven times stronger whenthe flanking A-tracts are positioned out-of-phase with the TG-motif than it is when the A-tracts are positioned in-phase with the TG-motif, We demonstrate that this effect correlates with differences in DNA curvature and apparent histone octamer affinity. We conclude that DNA curvature influences the local histone-DNA contacts and hence the accessibility of the NF-1 site in a nucleosome context.

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Documento generato il 05/04/20 alle ore 03:19:25