Do protein motifs read the histone code?
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.
de la Cruz
Xavier
X
Institut Català per la Recerca i Estudis Avançats, Barcelona, Spain.
Lois
Sergio
S
Sánchez-Molina
Sara
S
Martínez-Balbás
Marian A
MA
D000255:Adenosine Triphosphate / Q000737:chemistry; D020816:Amino Acid Motifs; D000818:Animals; D002843:Chromatin / Q000737:chemistry / Q000378:metabolism; D002875:Chromosomes / Q000378:metabolism; D006657:Histones / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008745:Methylation; D008954:Models, Biological; D008958:Models, Molecular; D010766:Phosphorylation; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D013329:Structure-Activity Relationship
D002843:Chromatin; D006657:Histones; D000255:Adenosine Triphosphate