Bromodomains in living cells participate in deciphering the histone code

Alejandra Loyola; Genevieve Almouzni

doi:10.1016/j.tcb.2004.04.005

Bromodomains in living cells participate in deciphering the histone code

Alejandra Loyola
, Genevieve Almouzni^*

^*Corresponding author for this work

Section de Recherche

Research output: Contribution to journal › Short survey › peer-review

33 Scopus citations

Abstract

The bromodomain, a module of ∼110 amino acids, is found in several chromatin-associated proteins, including histone acetyltransferases and chromatin-remodeling factors, and can bind to acetylated lysines. Such post-translational modifications occur mainly in the N-terminal tail of the histone proteins and, in combination with other modifications, are thought to participate in defining a histone code. Recent findings provide a model for how bromodomain-containing proteins participate in the recognition of acetylated histones.

Original language	English
Pages (from-to)	279-281
Number of pages	3
Journal	Trends in Cell Biology
Volume	14
Issue number	6
DOIs	https://doi.org/10.1016/j.tcb.2004.04.005
State	Published - 2004
Externally published	Yes

Bibliographical note

Funding Information:
We thank Andreas Ladurner, Edith Heard and Patricia Le-Baccon for insightful comments. A.L. was supported by an Institut Curie fellowship and then an EMBO fellowship (ALTF 635-2003). G.A.'s team is supported by a collaborative program between the Curie Institute and the Commissariat à l'Energie Atomique (PIC Paramètres Epigénétiques); la Ligue Nationale contre le Cancer (Equipe labellisée la Ligue); Euratom (FIGH-CT-1999–00010 and FIGH-CT-2002–00207); the Commissariat à l'Energie Atomique (LRC no. 26); and European Contracts RTN (HPRN-CT-2000–00078 and HPRN-CT-2002–00238).

ASJC Scopus subject areas

Cell Biology

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10.1016/j.tcb.2004.04.005

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title = "Bromodomains in living cells participate in deciphering the histone code",

abstract = "The bromodomain, a module of ∼110 amino acids, is found in several chromatin-associated proteins, including histone acetyltransferases and chromatin-remodeling factors, and can bind to acetylated lysines. Such post-translational modifications occur mainly in the N-terminal tail of the histone proteins and, in combination with other modifications, are thought to participate in defining a histone code. Recent findings provide a model for how bromodomain-containing proteins participate in the recognition of acetylated histones.",

author = "Alejandra Loyola and Genevieve Almouzni",

note = "Funding Information: We thank Andreas Ladurner, Edith Heard and Patricia Le-Baccon for insightful comments. A.L. was supported by an Institut Curie fellowship and then an EMBO fellowship (ALTF 635-2003). G.A.'s team is supported by a collaborative program between the Curie Institute and the Commissariat {\`a} l'Energie Atomique (PIC Param{\`e}tres Epig{\'e}n{\'e}tiques); la Ligue Nationale contre le Cancer (Equipe labellis{\'e}e la Ligue); Euratom (FIGH-CT-1999–00010 and FIGH-CT-2002–00207); the Commissariat {\`a} l'Energie Atomique (LRC no. 26); and European Contracts RTN (HPRN-CT-2000–00078 and HPRN-CT-2002–00238).",

year = "2004",

month = jun,

doi = "10.1016/j.tcb.2004.04.005",

language = "English",

volume = "14",

pages = "279--281",

journal = "Trends in Cell Biology",

issn = "0962-8924",

publisher = "Elsevier Ltd.",

number = "6",

}

TY - JOUR

T1 - Bromodomains in living cells participate in deciphering the histone code

AU - Loyola, Alejandra

AU - Almouzni, Genevieve

N1 - Funding Information: We thank Andreas Ladurner, Edith Heard and Patricia Le-Baccon for insightful comments. A.L. was supported by an Institut Curie fellowship and then an EMBO fellowship (ALTF 635-2003). G.A.'s team is supported by a collaborative program between the Curie Institute and the Commissariat à l'Energie Atomique (PIC Paramètres Epigénétiques); la Ligue Nationale contre le Cancer (Equipe labellisée la Ligue); Euratom (FIGH-CT-1999–00010 and FIGH-CT-2002–00207); the Commissariat à l'Energie Atomique (LRC no. 26); and European Contracts RTN (HPRN-CT-2000–00078 and HPRN-CT-2002–00238).

PY - 2004/6

Y1 - 2004/6

N2 - The bromodomain, a module of ∼110 amino acids, is found in several chromatin-associated proteins, including histone acetyltransferases and chromatin-remodeling factors, and can bind to acetylated lysines. Such post-translational modifications occur mainly in the N-terminal tail of the histone proteins and, in combination with other modifications, are thought to participate in defining a histone code. Recent findings provide a model for how bromodomain-containing proteins participate in the recognition of acetylated histones.

AB - The bromodomain, a module of ∼110 amino acids, is found in several chromatin-associated proteins, including histone acetyltransferases and chromatin-remodeling factors, and can bind to acetylated lysines. Such post-translational modifications occur mainly in the N-terminal tail of the histone proteins and, in combination with other modifications, are thought to participate in defining a histone code. Recent findings provide a model for how bromodomain-containing proteins participate in the recognition of acetylated histones.

UR - https://www.scopus.com/pages/publications/2942709639

U2 - 10.1016/j.tcb.2004.04.005

DO - 10.1016/j.tcb.2004.04.005

M3 - Short survey

C2 - 15183183

AN - SCOPUS:2942709639

SN - 0962-8924

VL - 14

SP - 279

EP - 281

JO - Trends in Cell Biology

JF - Trends in Cell Biology

IS - 6

ER -

Bromodomains in living cells participate in deciphering the histone code

Abstract

Bibliographical note

ASJC Scopus subject areas

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