English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/52071
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:

Characterization of structural variability sheds light on the specificity determinants of the interaction between effector domains and histone tails

AutorLois, Sergi; Akizu, Naiara; Mas de Xaxars, Gemma; Vázquez, Iago; Martínez-Balbás, Marian ; Cruz, Xavier de la
Palabras claveEpigenetic regulator specificity
Histone binding mode
Histone disorder
Histone-effector interaction
Lysine post-translational modifications
Modification of histone tails
Fecha de publicación2010
EditorLandes Bioscience
Taylor & Francis
CitaciónEpigenetics 5(2): 137-148 (2010)
ResumenStructural characterization of the interaction between histone tails and effector modules (bromodomains, chromodo-mains, PHD fingers, etc.) is fundamental to understand the mechanistic aspects of epigenetic regulation of gene expression. In recent years many researchers have applied this approach to specific systems, thus providing a valuable but fragmentary view of the histone-effector interaction. In our work we use this information to characterize the structural features of the two main components of this interaction, histone peptides and the binding site of effector domains (focusing on those which target modified lysines), and increase our knowledge on its specificity determinants. Our results show that the binding sites of effectors are structurally variable, but some clear trends allow their classification in three main groups: flat-groove, narrow-groove and cavity-insertion. In addition, we found that even within these classes binding site variability is substantial. These results in context with the work from other researchers indicate that the there are at least two determinants of binding specificity in the binding site of effector modules. Finally, our analysis of the histone peptides sheds light on the structural transition experienced by histone tails upon effector binding, showing that it may vary depending on the local properties of the sequence stretch considered, thus allowing us to identify an additional specificity determinant for this interaction. Overall, the results of our analysis contribute to clarify the origins of specificity: different regions of the binding site and, in particular, differences in the disorder-order transitions experienced by different histone sequence stretches upon binding. © 2010 Landes Bioscience.
Versión del editorhttp://dx.doi.org/10.4161/epi.5.2.11079
Identificadoresdoi: 10.4161/epi.5.2.11079
issn: 1559-2294
e-issn: 1559-2308
Aparece en las colecciones: (IBMB) Artículos
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
accesoRestringido.pdf15,38 kBAdobe PDFVista previa
Mostrar el registro completo

Artículos relacionados:

NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.