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The bromodomain of Gcn5p interacts in vitro with specific residues in the N terminus of histone H4. (Articolo in rivista)
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- The bromodomain of Gcn5p interacts in vitro with specific residues in the N terminus of histone H4. (Articolo in rivista) (literal)
- Anno
- 1999-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1006/jmbi.1999.2577 (literal)
- Alternative label
Ornaghi P, Ballario P, Lena AM, González A, Filetici P (1999)
The bromodomain of Gcn5p interacts in vitro with specific residues in the N terminus of histone H4.
in Journal of molecular biology (Online); Academic Press, London (Regno Unito)
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- Ornaghi P, Ballario P, Lena AM, González A, Filetici P (literal)
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- http://www.sciencedirect.com/science/article/pii/S0022283699925779 (literal)
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- Departamento de Genetica Molecular, Instituto de Fisiologia Celular, Universidad Nacional Autonoma de Mexico Dipartimento di Genetica e Biologia Molecolare Universita La Sapienza (literal)
- Titolo
- The bromodomain of Gcn5p interacts in vitro with specific residues in the N terminus of histone H4. (literal)
- Abstract
- Whereas the histone acetyltransferase activity of yeast Gcn5p has been
widely studied, its structural interactions with the histones and the role
of the carboxy-terminal bromodomain are still unclear. Using a glutathione
S-transferase pull down assay we show that Gcn5p binds the
amino-terminal tails of histones H3 and H4, but not H2A and H2B. The
deletion of bromodomain abolishes this interaction and bromodomain
alone is able to interact with the H3 and H4 N termini. The amino acid
residues of the H4 N terminus involved in the binding with Gcn5p have
been studied by site-directed mutagenesis. The substitution of amino acid
residues R19 or R23 of the H4 N terminus with a glutamine (Q) abolishes
the interaction with Gcn5p and the bromodomain. These residues differ
from those known to be acetylated or to be involved in binding the SIR
proteins. This evidence and the known dispensability of the bromodomain
for Gcn5p acetyltransferase activity suggest a new structural role
for the highly evolutionary conserved bromodomain. (literal)
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