English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/121771
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:

Title

Do protein motifs read the histone code?

AuthorsCruz, Xavier de la ; Lois, Sergi; Sánchez-Molina, Sara; Martínez-Balbás, Marian
Issue Date21-Jan-2005
PublisherWiley-VCH
CitationBioEssays 27(2): 164-175 (2005)
AbstractThe existence of different patterns of chemical modifications (acetylation, methylation, phosphorylation, ubiquitination and ADP-ribosylation) of the histone tails led, some years ago, to the histone code hypothesis. According to this hypothesis, these modifications would provide binding sites for proteins that can change the chromatin state to either active or repressed. Interestingly, some protein domains present in histone-modifying enzymes are known to interact with these covalent marks in the histone tails. This was first shown for the bromodomain, which was found to interact selectively with acetylated lysines at the histone tails. More recently, it has been described that the chromodomain can be targeted to methylation marks in histone N-terminal domains. Finally, the interaction between the SANT domain and histones is also well documented. Overall, experimental evidence suggests that these domains could be involved in the recruitment of histone-modifying enzymes to discrete chromosomal locations, and/or in the regulation their enzymatic activity. Within this context, we review the distribution of bromodomains, chromodomains and SANT domains among chromatin-modifying enzymes and discuss how they can contribute to the translation of the histone code. © 2005 Wiley Periodicals, Inc.
Publisher version (URL)http://dx.doi.org/10.1002/bies.20176
URIhttp://hdl.handle.net/10261/121771
DOI10.1002/bies.20176
Identifiersdoi: 10.1002/bies.20176
issn: 0265-9247
Appears in Collections:(CID) Artículos
(IBMB) Artículos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdf15,38 kBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.