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Titolo:
Poly(dA center dot dT) sequences exist as rigid DNA structures in nucleosome-free yeast promoters in vivo
Autore:
Suter, B; Schnappauf, G; Thoma, F;
Indirizzi:
ETH Zurich, Inst Zellbiol, CH-8093 Zurich, Switzerland ETH Zurich ZurichSwitzerland CH-8093 lbiol, CH-8093 Zurich, Switzerland
Titolo Testata:
NUCLEIC ACIDS RESEARCH
fascicolo: 21, volume: 28, anno: 2000,
pagine: 4083 - 4089
SICI:
0305-1048(20001101)28:21<4083:PCDDSE>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEOTIDE EXCISION-REPAIR; THYMINE DIMER FORMATION; SACCHAROMYCES-CEREVISIAE; CHROMATIN STRUCTURE; BINDING PROTEIN; IN-VIVO; BIOLOGICAL IMPLICATIONS; NONTRANSCRIBED STRAND; POSITIONED NUCLEOSOME; PYRIMIDINE DIMERS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
54
Recensione:
Indirizzi per estratti:
Indirizzo: Thoma, F ETH Zurich, Inst Zellbiol, CH-8093 Zurich, Switzerland ETH Zurich Zurich Switzerland CH-8093 -8093 Zurich, Switzerland
Citazione:
B. Suter et al., "Poly(dA center dot dT) sequences exist as rigid DNA structures in nucleosome-free yeast promoters in vivo", NUCL ACID R, 28(21), 2000, pp. 4083-4089

Abstract

Poly(dA.dT) sequences (T-tracts) are abundant genomic DNA elements with unusual properties in vitro and an established role in transcriptional regulation of yeast genes. In vitro T-tracts are rigid, contribute to DNA bending, affect assembly in nucleosomes and generate a characteristic pattern of CPDs (cyclobutane pyrimidine dimers) upon irradiation with UV light (UV photofootprint). in eukaryotic cells, where DNA is packaged in chromatin, the DNA structure of T-tracts is unknown. Here we have used in vivo UV photofootprinting and DNA repair by photolyase to investigate the structure and accessibility of T-tracts in yeast promoters (HIS3, URA3 and ILV1). The same characteristic photofootprints were obtained in yeast and in naked DNA, demonstrating that the unusual T-tract structure exists in living cells. Rapid repair of CPDs in the T-tracts demonstrates that these T-tracts were not folded in nucleosomes, Moreover, neither datin, a T-tract binding protein, norGcn5p, a histone acetyltransferase involved in nucleosome remodelling, showed an influence on the structure and accessibility of T-tracts. The data support a contribution of this unusual DNA structure to transcriptional regulation.

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Documento generato il 03/06/20 alle ore 00:03:21