Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1.

Détails

ID Serval
serval:BIB_7406051D405C
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1.
Périodique
Genes and Development
Auteur⸱e⸱s
Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.
ISSN
0890-9369[print], 0890-9369[linking]
Statut éditorial
Publié
Date de publication
2003
Volume
17
Numéro
7
Pages
896-911
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, U.S. Gov't, P.H.S.
Publication Status: ppublish
Résumé
The abundant and chromatin-associated protein HCF-1 is a critical player in mammalian cell proliferation as well as herpes simplex virus (HSV) transcription. We show here that separate regions of HCF-1 critical for its role in cell proliferation associate with the Sin3 histone deacetylase (HDAC) and a previously uncharacterized human trithorax-related Set1/Ash2 histone methyltransferase (HMT). The Set1/Ash2 HMT methylates histone H3 at Lys 4 (K4), but not if the neighboring K9 residue is already methylated. HCF-1 tethers the Sin3 and Set1/Ash2 transcriptional regulatory complexes together even though they are generally associated with opposite transcriptional outcomes: repression and activation of transcription, respectively. Nevertheless, this tethering is context-dependent because the transcriptional activator VP16 selectively binds HCF-1 associated with the Set1/Ash2 HMT complex in the absence of the Sin3 HDAC complex. These results suggest that HCF-1 can broadly regulate transcription, both positively and negatively, through selective modulation of chromatin structure.
Mots-clé
Binding Sites, Cell Division/physiology, DNA-Binding Proteins/genetics, Hela Cells, Herpes Simplex Virus Protein Vmw65/metabolism, Histone Deacetylases/genetics, Histone Deacetylases/isolation &amp, purification, Histone-Lysine N-Methyltransferase, Host Cell Factor C1, Humans, Kinetics, Methyltransferases/genetics, Protein Methyltransferases, Proteins/metabolism, Saccharomyces cerevisiae Proteins/genetics, Sin3 Histone Deacetylase and Corepressor Complex, Transcription Factors/genetics, Transfection
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 15:36
Dernière modification de la notice
20/08/2019 14:31
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