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

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 machiner...

Full description

Saved in:
Bibliographic Details
Published in:Nucleic acids research 2017-02, Vol.45 (4), p.2150-2165
Main Authors: González-Arzola, Katiuska, Díaz-Quintana, Antonio, Rivero-Rodríguez, Francisco, Velázquez-Campoy, Adrián, De la Rosa, Miguel A, Díaz-Moreno, Irene
Format: Article
Language:English
Subjects:
Arabidopsis
Arabidopsis Proteins - chemistry
Arabidopsis Proteins - metabolism
Cells, Cultured
Chromatin - genetics
Chromatin - metabolism
Cytochromes c - chemistry
Cytochromes c - metabolism
DNA Damage
Histone Chaperones - chemistry
Histone Chaperones - metabolism
Histones - metabolism
Humans
Models, Molecular
Nucleosomes - metabolism
Plant Cells
Protein Binding
Protein Conformation
Protein Interaction Domains and Motifs
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Structural Biology
Thermodynamics
Transcription Factors - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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 obtained indicate that the underlying molecular mechanisms in nucleosome disassembly/reassembly are highly conserved throughout evolution, as inferred from the similar inhibition of plant NRP1 and human SET/TAF-Iβ by cytochrome c during DNA damage response.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/gkw1215