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Titolo:
Recruitment of the RNA polymerase II holoenzyme and its implications in gene regulation
Autore:
Barberis, A; Gaudreau, L;
Indirizzi:
Univ Zurich, Inst Mol Biol, CH-8057 Zurich, Switzerland Univ Zurich Zurich Switzerland CH-8057 Biol, CH-8057 Zurich, Switzerland Sloan Kettering Canc Inst, Program Mol Biol, New York, NY 10021 USA Sloan Kettering Canc Inst New York NY USA 10021 l, New York, NY 10021 USA
Titolo Testata:
BIOLOGICAL CHEMISTRY
fascicolo: 12, volume: 379, anno: 1998,
pagine: 1397 - 1405
SICI:
1431-6730(199812)379:12<1397:ROTRPI>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSCRIPTIONAL ACTIVATION DOMAIN; TATA-BINDING PROTEIN; SACCHAROMYCES-CEREVISIAE; CHROMATIN STRUCTURE; PHO5 PROMOTER; NUCLEOSOME DISRUPTION; DROSOPHILA EMBRYO; FACTOR-TFIIB; COMPLEX; YEAST;
Keywords:
chromatin; RNA polymerase II holoenzyme; transcriptional activation by recruitment;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
82
Recensione:
Indirizzi per estratti:
Indirizzo: Barberis, A UnivdZurich, Inst Mol Biol, Winterthurerstr 190, CH-8057 Zurich, Switzerlan Univ Zurich Winterthurerstr 190 Zurich Switzerland CH-8057 an
Citazione:
A. Barberis e L. Gaudreau, "Recruitment of the RNA polymerase II holoenzyme and its implications in gene regulation", BIOL CHEM, 379(12), 1998, pp. 1397-1405

Abstract

In yeast cells, interaction between a DNA-bound protein and a single component of the RNA polymerase II (poIII) holoenzyme is sufficient to recruit the latter to a promoter and thereby activate gene transcription. Here we review results which have suggested such a simple mechanism for how genes canbe turned on. The series of experiments which eventually led to this modelwas originally instigated by studying gene expression in a yeast strain which carries a point mutation in Gal11, a component of the poIII holoenzyme. In cells containing this mutant protein termed Gal11P, a derivative of thetranscriptional activator Gal4 devoid of any classical activating region is turned into a strong activator. This activating function acquired by an otherwise silent DNA-binding protein is solely due to a novel and fortuitousinteraction between Gal11P and a fragment of the Ga14 dimerization region generated by the P mutation. The simplest explanation for these results is that tethering Gal11 to DNA recruits the poIII holoenzyme and, consequently, activates gene transcription. Transcription factors that are believed notto be integral part of the poIII holoenzyme but are nevertheless required for this instance of gene activation, e.g, the TATA-binding TFIID complex, may bind DNA cooperatively with the holoenzyme when recruited to a promoter, thus forming a complete poIII preinitiation complex. One prediction of this model is that recruitment of the entire poIII transcription complex and consequent gene activation can be achieved by tethering different components to DNA. Indeed, fusion of a DNA-binding domain to a variety of poIII holoenzyme components and TFIID subunits leads to activation of genes bearing the recognition site for the DNA-binding protein. These results imply that accessory factors, which are required to remove or modify nucleosomes do notneed to be directly contacted by activators, but can rather be engaged in the activation process when the poIII complex is recruited to DNA. In fact,recruitment of the poIII holoenzyme suffices to remodel nucleosomes at thePHO5 promoter and presumably at many other promoters. Other events in the process of gene expression following recruitment of the transcription complex, e.g. initiation, promoter clearance, elongation and termination, could unravel as a consequence of the recruitment step and the formation of an active preinitiation complex on DNA. This view does not exclude the possibility that classical activators also act directly on chromatin remodeling and post-recruitment steps to regulate gene expression.

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Documento generato il 20/09/20 alle ore 04:28:31