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

ABSTRACT: 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 cytoc

SUBMITTER: Gonzalez-Arzola K 

PROVIDER: S-EPMC5389710 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature