Histone chaperone-mediated nucleosome assembly process

A huge amount of information is stored in genomic DNA and this stored information resides inside the nucleus with the aid of chromosomal condensation factors. It has been reported that the repeat nucleosome core particle (NCP) consists of 147-bp of DNA and two copies of H2A, H2B, H3 and H4. Regulati...

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Bibliographic Details
Published in:PloS one 2015-01, Vol.10 (1), p.e0115007-e0115007
Main Authors: Fan, Hsiu-Fang, Liu, Zi-Ning, Chow, Sih-Yao, Lu, Yi-Han, Li, Hsin
Format: Article
Language:English
Subjects:
Analysis
Assembly
Cell cycle
Cell Cycle Proteins - chemistry
Cell Cycle Proteins - metabolism
Chaperones
Chromatin
Chromosomes
Condensates
Deoxyribonucleic acid
DNA
Enthalpy
Gene expression
Genomes
Histones
Laboratories
Life sciences
Molecular Chaperones - chemistry
Molecular Chaperones - metabolism
Nuclei
Nucleosome Assembly Protein 1 - chemistry
Nucleosome Assembly Protein 1 - metabolism
Nucleosomes - chemistry
Nucleosomes - metabolism
Particle motion
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - metabolism
Substrates
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Summary:A huge amount of information is stored in genomic DNA and this stored information resides inside the nucleus with the aid of chromosomal condensation factors. It has been reported that the repeat nucleosome core particle (NCP) consists of 147-bp of DNA and two copies of H2A, H2B, H3 and H4. Regulation of chromosomal structure is important to many processes inside the cell. In vivo, a group of histone chaperones facilitate and regulate nucleosome assembly. How NCPs are constructed with the aid of histone chaperones remains unclear. In this study, the histone chaperone-mediated nucleosome assembly process was investigated using single-molecule tethered particle motion (TPM) experiments. It was found that Asf1 is able to exert more influence than Nap1 and poly glutamate acid (PGA) on the nucleosome formation process, which highlights Asf1's specific role in tetrasome formation. Thermodynamic parameters supported a model whereby energetically favored nucleosomal complexes compete with non-nucleosomal complexes. In addition, our kinetic findings propose the model that histone chaperones mediate nucleosome assembly along a path that leads to enthalpy-favored products with free histones as reaction substrates.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0115007