A bromodomain–DNA interaction facilitates acetylation-dependent bivalent nucleosome recognition by the BET protein BRDT

A bromodomain–DNA interaction facilitates acetylation-dependent bivalent nucleosome recognition by the BET protein BRDT

Many chromatin modifying proteins, including BRDT, contain bromodomains, which are known to interact with nucleosomes. Here, the authors find that BRDT interacts with nucleosomes via only one of its two bromodomains, and that the interaction involves contacts with DNA as well as acetylated histones.

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Autores principales: Thomas C. R. Miller, Bernd Simon, Vladimir Rybin, Helga Grötsch, Sandrine Curtet, Saadi Khochbin, Teresa Carlomagno, Christoph W. Müller
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2016
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Acceso en línea:https://doaj.org/article/c93aafea18804c96b630d1d51ba32d60
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spelling oai:doaj.org-article:c93aafea18804c96b630d1d51ba32d602021-12-02T17:33:20ZA bromodomain–DNA interaction facilitates acetylation-dependent bivalent nucleosome recognition by the BET protein BRDT10.1038/ncomms138552041-1723https://doaj.org/article/c93aafea18804c96b630d1d51ba32d602016-12-01T00:00:00Zhttps://doi.org/10.1038/ncomms13855https://doaj.org/toc/2041-1723Many chromatin modifying proteins, including BRDT, contain bromodomains, which are known to interact with nucleosomes. Here, the authors find that BRDT interacts with nucleosomes via only one of its two bromodomains, and that the interaction involves contacts with DNA as well as acetylated histones.Thomas C. R. MillerBernd SimonVladimir RybinHelga GrötschSandrine CurtetSaadi KhochbinTeresa CarlomagnoChristoph W. MüllerNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-13 (2016)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Thomas C. R. Miller
Bernd Simon
Vladimir Rybin
Helga Grötsch
Sandrine Curtet
Saadi Khochbin
Teresa Carlomagno
Christoph W. Müller
A bromodomain–DNA interaction facilitates acetylation-dependent bivalent nucleosome recognition by the BET protein BRDT
description Many chromatin modifying proteins, including BRDT, contain bromodomains, which are known to interact with nucleosomes. Here, the authors find that BRDT interacts with nucleosomes via only one of its two bromodomains, and that the interaction involves contacts with DNA as well as acetylated histones.
format article
author Thomas C. R. Miller
Bernd Simon
Vladimir Rybin
Helga Grötsch
Sandrine Curtet
Saadi Khochbin
Teresa Carlomagno
Christoph W. Müller
author_facet Thomas C. R. Miller
Bernd Simon
Vladimir Rybin
Helga Grötsch
Sandrine Curtet
Saadi Khochbin
Teresa Carlomagno
Christoph W. Müller
author_sort Thomas C. R. Miller
title A bromodomain–DNA interaction facilitates acetylation-dependent bivalent nucleosome recognition by the BET protein BRDT
title_short A bromodomain–DNA interaction facilitates acetylation-dependent bivalent nucleosome recognition by the BET protein BRDT
title_full A bromodomain–DNA interaction facilitates acetylation-dependent bivalent nucleosome recognition by the BET protein BRDT
title_fullStr A bromodomain–DNA interaction facilitates acetylation-dependent bivalent nucleosome recognition by the BET protein BRDT
title_full_unstemmed A bromodomain–DNA interaction facilitates acetylation-dependent bivalent nucleosome recognition by the BET protein BRDT
title_sort bromodomain–dna interaction facilitates acetylation-dependent bivalent nucleosome recognition by the bet protein brdt
publisher Nature Portfolio
publishDate 2016
url https://doaj.org/article/c93aafea18804c96b630d1d51ba32d60
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