2024-03-28T11:41:45Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/1217712019-03-18T15:14:44Zcom_10261_76com_10261_5com_10261_41com_10261_1col_10261_329col_10261_294
Cruz, Xavier de la
Lois, Sergi
Sánchez-Molina, Sara
Martínez-Balbás, Marian
2015-09-08T09:45:39Z
2015-09-08T09:45:39Z
2005-01-21
BioEssays 27(2): 164-175 (2005)
http://hdl.handle.net/10261/121771
10.1002/bies.20176
The 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.
eng
closedAccess
Do protein motifs read the histone code?
artículo