Naslov
Differential cofactor requirements for histone eviction from two nucleosomes at the yeast PHO84 promoter

Autori
Korber, Philipp ; Silić Krstulović, Bojana ; Blaschke, Dorothea ; Wippo, Christian J. ; Ertel, Franziska ; Stürzl, Sabrina ; Barbarić, Slobodan

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
Book of Abstracts of Congress of the Croatian Society of Biochemistry and Molecular Biology / Strelec, Ivica ; Glavaš-Obrovac, Ljubica - Osijek : Grafika Osijek, 2008, 131-131

ISBN
978-953-95551-2-0

Skup
Congress of the Croatian Society of Biochemistry and Molecular Biology

Mjesto i datum
Osijek, Hrvatska, 17.09.2008. - 20.09.2008

Vrsta sudjelovanja
Poster

Vrsta recenzije
Domaća recenzija

Ključne riječi
chromatin remodeling; transcriptional regulation; yeast PHO genes

Sažetak
The mechanisms, which cell has evolved, to modulate the chromatin structure and consequently gene expression were extensively studied at the yeast PHO5 and PHO8 genes. In order to get further insight into this issue, we started to study the yeast PHO84 promoter, which is coregulated with the PHO5 and PHO8 promoters by the phosphate availability and is the strongest PHO promoter. In the repressed state this promoter exhibits a short hypersensitive region flanked by two positioned nucleosomes and harbouring two high affinity Pho4 binding sites. Upon induction, the chromatin structure is remodeled into an extensive hypersensitive region that allows access to two additional UASp elements. This chromatin transition is strongly dependent on Snf2, Ino80 and Gcn5. Interestingly, the two nucleosomes show a markedly different degree of cofactor requirement: remodeling of the upstream is critically dependent on Snf2, while remodeling of the downstream is only stimulated by this cofactor. We also showed that remodeling of the upstream nucleosome is more dependent on Ino80, but this cofactor is, however, not essentially required for complete remodeling of the downstream nucleosome upon full induction, even in the absence of Snf2. Chromatin remodeling at the PHO84 promoter leads to the eviction of histones from the promoter, so we also examined a possible role of histone chaperone Asf1 for the activation of this promoter, and found that this protein has a stimulating but not essential role in PHO84 promoter induction, less pronounced than at the PHO5 promoter. Moreover, at the PHO84 promoter, but also at the PHO5 promoter, Asf1 likely functions through its essential action on the histone acetyltransferase Rtt109, which acetylates histone H3 at lysine 56.

Izvorni jezik
Engleski

Znanstvena područja
Biotehnologija

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