http://www.cnr.it/ontology/cnr/individuo/prodotto/ID11412
H4 acetylation does not replace H3 acetylation in chromatin remodelling and transcription activation of Adr1-dependent genes. (Articolo in rivista)
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- Label
- H4 acetylation does not replace H3 acetylation in chromatin remodelling and transcription activation of Adr1-dependent genes. (Articolo in rivista) (literal)
- Anno
- 2006-01-01T00:00:00+01:00 (literal)
- Alternative label
Eleonora Agricola,1+; Loredana Verdone,2+; Ernesto Di Mauro1,2; and Micaela Caserta2* (2006)
H4 acetylation does not replace H3 acetylation in chromatin remodelling and transcription activation of Adr1-dependent genes.
in Molecular microbiology (Print)
(literal)
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- Eleonora Agricola,1+; Loredana Verdone,2+; Ernesto Di Mauro1,2; and Micaela Caserta2* (literal)
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- 1Istituto Pasteur-Fondazione Cenci Bolognetti, c/o
Dipartimento di Genetica e Biologia Molecolare,
Università La Sapienza, 00185 Rome, Italy.
2Istituto Biologia e Patologia Molecolari, CNR, 00185
Rome, Italy. (literal)
- Titolo
- H4 acetylation does not replace H3 acetylation in chromatin remodelling and transcription activation of Adr1-dependent genes. (literal)
- Abstract
- Histone acetylation regulates gene expression.
Whether this is caused by a general increase in
nucleosome fluidity due to charge neutralization or by
a more specific code is still matter of debate. By using
a set of glucose-repressed Adr1-dependent genes of
Saccharomyces cerevisiae, whose transcription was
previously shown to require both Gcn5 and Esa1, we
asked how changes of histone acetylation patterns
at the promoter nucleosomes regulate chromatin
remodelling and activation. When the signal of
glucose reduction reaches the cells, H4 acetylation is
kept constant while an increase of H3 acetylation
occurs, in an Adr1- and Gcn5-dependent manner.
In cells lacking Gcn5 activity, the H3 acetylation
increase does not occur and an unexpected increase
of histone H4 acetylation is observed. Nevertheless,
chromatin remodelling and transcription activation
are impaired, suggesting that acetylation of H3 and
H4 histones plays different roles. (literal)
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