Structural studies on MRG701 chromodomain reveal a novel dimerization interface of MRG proteins in green plants
Protein & Cell
;
(12): 792-803, 2016.
Artículo
en Inglés
| WPRIM
| ID: wpr-757369
ABSTRACT
MRG proteins are conserved during evolution in fungi, flies, mammals and plants, and they can exhibit diversified functions. The animal MRGs were found to form various complexes to activate gene expression. Plant MRG1/2 and MRG702 were reported to be involved in the regulation of flowering time via binding to H3K36me3-marked flowering genes. Herein, we determined the crystal structure of MRG701 chromodomain (MRG701). MRG701 forms a novel dimerization fold both in crystal and in solution. Moreover, we found that the dimerization of MRG chromodomains is conserved in green plants. Our findings may provide new insights into the mechanism of MRGs in regulation of gene expression in green plants.
Texto completo:
Disponible
Índice:
WPRIM (Pacífico Occidental)
Asunto principal:
Péptidos
/
Unión Proteica
/
Oryza
/
Sitios de Unión
/
Proteínas Recombinantes
/
Proteínas Cromosómicas no Histona
/
Histonas
/
Modelos Moleculares
/
Expresión Génica
/
Química
Tipo de estudio:
Estudio pronóstico
Idioma:
Inglés
Revista:
Protein & Cell
Año:
2016
Tipo del documento:
Artículo
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