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Histone chaperone activity of Arabidopsis thaliana NRP1 is blocked by cytochrome c

Opened Access Histone chaperone activity of Arabidopsis thaliana NRP1 is blocked by cytochrome c

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Autor: González Arzola, Katiuska
Díaz Quintana, Antonio
Rivero Rodríguez, Francisco
Velázquez Campoy, Adrián
Rosa, Miguel A. de la
Díaz Moreno, Irene
Fecha: 2017
Publicado en: Nucleic Acids Research, 45 (4), 2150-2165.
Tipo de documento: Artículo
Resumen: Higher-order plants and mammals use similar mechanisms to repair and tolerate oxidative DNA damage. Most studies on the DNA repair process have focused on yeast and mammals, in which histone chaperone-mediated nucleosome disassembly/reassembly is essential for DNA to be accessible to repair machinery. However, little is known about the specific role and modulation of histone chaperones in the context of DNA damage in plants. Here, the histone chaperone NRP1, which is closely related to human SET/TAF-Iβ, was found to exhibit nucleosome assembly activity in vitro and to accumulate in the chromatin of Arabidopsis thaliana after DNA breaks. In addition, this work establishes that NRP1 binds to cytochrome c, thereby preventing the former from binding to histones. Since NRP1 interacts with cytochrome c at its earmuff domain, that is, its histone-binding domain, cytochrome c thus competes with core histones and hampers the activity of NRP1 as a histone chaperone. Altogether, the results obta...
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Cita: González Arzola, K., Díaz Quintana, A., Rivero Rodríguez, F., Velázquez Campoy, A., Rosa, M.A.d.l. y Díaz Moreno, I. (2017). Histone chaperone activity of Arabidopsis thaliana NRP1 is blocked by cytochrome c. Nucleic Acids Research, 45 (4), 2150-2165.
Tamaño: 5.752Mb
Formato: PDF

URI: http://hdl.handle.net/11441/64082

DOI: 0.1093/nar/gkw1215

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