Multivalent engagement of TFIID to nucleosomes.

The process of eukaryotic transcription initiation involves the assembly of basal transcription factor complexes on the gene promoter. The recruitment of TFIID is an early and important step in this process. Gene promoters contain distinct DNA sequence elements and are marked by the presence of post...

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Autores principales:	Rick van Nuland, Andrea W Schram, Frederik M A van Schaik, Pascal W T C Jansen, Michiel Vermeulen, H T Marc Timmers
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/699b6a3a255c428fa0548c29442c58b3
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spelling	oai:doaj.org-article:699b6a3a255c428fa0548c29442c58b32021-11-18T08:55:48ZMultivalent engagement of TFIID to nucleosomes.1932-620310.1371/journal.pone.0073495https://doaj.org/article/699b6a3a255c428fa0548c29442c58b32013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24039962/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203The process of eukaryotic transcription initiation involves the assembly of basal transcription factor complexes on the gene promoter. The recruitment of TFIID is an early and important step in this process. Gene promoters contain distinct DNA sequence elements and are marked by the presence of post-translationally modified nucleosomes. The contributions of these individual features for TFIID recruitment remain to be elucidated. Here, we use immobilized reconstituted promoter nucleosomes, conventional biochemistry and quantitative mass spectrometry to investigate the influence of distinct histone modifications and functional DNA-elements on the binding of TFIID. Our data reveal synergistic effects of H3K4me3, H3K14ac and a TATA box sequence on TFIID binding in vitro. Stoichiometry analyses of affinity purified human TFIID identified the presence of a stable dimeric core. Several peripheral TAFs, including those interacting with distinct promoter features, are substoichiometric yet present in substantial amounts. Finally, we find that the TAF3 subunit of TFIID binds to poised promoters in an H3K4me3-dependent manner. Moreover, the PHD-finger of TAF3 is important for rapid induction of target genes. Thus, fine-tuning of TFIID engagement on promoters is driven by synergistic contacts with both DNA-elements and histone modifications, eventually resulting in a high affinity interaction and activation of transcription.Rick van NulandAndrea W SchramFrederik M A van SchaikPascal W T C JansenMichiel VermeulenH T Marc TimmersPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 9, p e73495 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Rick van Nuland Andrea W Schram Frederik M A van Schaik Pascal W T C Jansen Michiel Vermeulen H T Marc Timmers Multivalent engagement of TFIID to nucleosomes.
description	The process of eukaryotic transcription initiation involves the assembly of basal transcription factor complexes on the gene promoter. The recruitment of TFIID is an early and important step in this process. Gene promoters contain distinct DNA sequence elements and are marked by the presence of post-translationally modified nucleosomes. The contributions of these individual features for TFIID recruitment remain to be elucidated. Here, we use immobilized reconstituted promoter nucleosomes, conventional biochemistry and quantitative mass spectrometry to investigate the influence of distinct histone modifications and functional DNA-elements on the binding of TFIID. Our data reveal synergistic effects of H3K4me3, H3K14ac and a TATA box sequence on TFIID binding in vitro. Stoichiometry analyses of affinity purified human TFIID identified the presence of a stable dimeric core. Several peripheral TAFs, including those interacting with distinct promoter features, are substoichiometric yet present in substantial amounts. Finally, we find that the TAF3 subunit of TFIID binds to poised promoters in an H3K4me3-dependent manner. Moreover, the PHD-finger of TAF3 is important for rapid induction of target genes. Thus, fine-tuning of TFIID engagement on promoters is driven by synergistic contacts with both DNA-elements and histone modifications, eventually resulting in a high affinity interaction and activation of transcription.
format	article
author	Rick van Nuland Andrea W Schram Frederik M A van Schaik Pascal W T C Jansen Michiel Vermeulen H T Marc Timmers
author_facet	Rick van Nuland Andrea W Schram Frederik M A van Schaik Pascal W T C Jansen Michiel Vermeulen H T Marc Timmers
author_sort	Rick van Nuland
title	Multivalent engagement of TFIID to nucleosomes.
title_short	Multivalent engagement of TFIID to nucleosomes.
title_full	Multivalent engagement of TFIID to nucleosomes.
title_fullStr	Multivalent engagement of TFIID to nucleosomes.
title_full_unstemmed	Multivalent engagement of TFIID to nucleosomes.
title_sort	multivalent engagement of tfiid to nucleosomes.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/699b6a3a255c428fa0548c29442c58b3
work_keys_str_mv	AT rickvannuland multivalentengagementoftfiidtonucleosomes AT andreawschram multivalentengagementoftfiidtonucleosomes AT frederikmavanschaik multivalentengagementoftfiidtonucleosomes AT pascalwtcjansen multivalentengagementoftfiidtonucleosomes AT michielvermeulen multivalentengagementoftfiidtonucleosomes AT htmarctimmers multivalentengagementoftfiidtonucleosomes
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Multivalent engagement of TFIID to nucleosomes.

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