Abstract
Histones are the protein components of the nucleosome, which forms the basic architecture of eukaryotic chromatin. Histones H2A, H2B, H3, and H4 are composed of two common regions, the "histone fold" and the "histone tail". Many efforts have been focused on the mechanisms by which the post-translational modifications of histone tails regulate the higher-order chromatin architecture. On the other hand, previous biochemical studies have suggested that histone tails also affect the structure and stability of the nucleosome core particle itself. However, the precise contributions of each histone tail are unclear. In the present study, we determined the crystal structures of four mutant nucleosomes, in which one of the four histones, H2A, H2B, H3, or H4, lacked the N-terminal tail. We found that the deletion of the H2B or H3 N-terminal tail affected histone-DNA interactions and substantially decreased nucleosome stability. These findings provide important information for understanding the complex roles of histone tails in regulating chromatin structure.
| Original language | English |
|---|---|
| Pages (from-to) | 363-369 |
| Number of pages | 7 |
| Journal | FEBS Open Bio |
| Volume | 3 |
| DOIs | |
| Publication status | Published - 2013 Aug |
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Keywords
- Chromatin
- Crystal structure
- Histone tail
- Nucleosome
- Thermal stability assay
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
Cite this
Contribution of histone N-terminal tails to the structure and stability of nucleosomes. / Iwasaki, Wakana; Miya, Yuta; Horikoshi, Naoki; Osakabe, Akihisa; Taguchi, Hiroyuki; Tachiwana, Hiroaki; Shibata, Takehiko; Kagawa, Wataru; Kurumizaka, Hitoshi.
In: FEBS Open Bio, Vol. 3, 08.2013, p. 363-369.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Contribution of histone N-terminal tails to the structure and stability of nucleosomes
AU - Iwasaki, Wakana
AU - Miya, Yuta
AU - Horikoshi, Naoki
AU - Osakabe, Akihisa
AU - Taguchi, Hiroyuki
AU - Tachiwana, Hiroaki
AU - Shibata, Takehiko
AU - Kagawa, Wataru
AU - Kurumizaka, Hitoshi
PY - 2013/8
Y1 - 2013/8
N2 - Histones are the protein components of the nucleosome, which forms the basic architecture of eukaryotic chromatin. Histones H2A, H2B, H3, and H4 are composed of two common regions, the "histone fold" and the "histone tail". Many efforts have been focused on the mechanisms by which the post-translational modifications of histone tails regulate the higher-order chromatin architecture. On the other hand, previous biochemical studies have suggested that histone tails also affect the structure and stability of the nucleosome core particle itself. However, the precise contributions of each histone tail are unclear. In the present study, we determined the crystal structures of four mutant nucleosomes, in which one of the four histones, H2A, H2B, H3, or H4, lacked the N-terminal tail. We found that the deletion of the H2B or H3 N-terminal tail affected histone-DNA interactions and substantially decreased nucleosome stability. These findings provide important information for understanding the complex roles of histone tails in regulating chromatin structure.
AB - Histones are the protein components of the nucleosome, which forms the basic architecture of eukaryotic chromatin. Histones H2A, H2B, H3, and H4 are composed of two common regions, the "histone fold" and the "histone tail". Many efforts have been focused on the mechanisms by which the post-translational modifications of histone tails regulate the higher-order chromatin architecture. On the other hand, previous biochemical studies have suggested that histone tails also affect the structure and stability of the nucleosome core particle itself. However, the precise contributions of each histone tail are unclear. In the present study, we determined the crystal structures of four mutant nucleosomes, in which one of the four histones, H2A, H2B, H3, or H4, lacked the N-terminal tail. We found that the deletion of the H2B or H3 N-terminal tail affected histone-DNA interactions and substantially decreased nucleosome stability. These findings provide important information for understanding the complex roles of histone tails in regulating chromatin structure.
KW - Chromatin
KW - Crystal structure
KW - Histone tail
KW - Nucleosome
KW - Thermal stability assay
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UR - http://www.scopus.com/inward/citedby.url?scp=84883781627&partnerID=8YFLogxK
U2 - 10.1016/j.fob.2013.08.007
DO - 10.1016/j.fob.2013.08.007
M3 - Article
C2 - 24251097
AN - SCOPUS:84883781627
VL - 3
SP - 363
EP - 369
JO - FEBS Open Bio
JF - FEBS Open Bio
SN - 2211-5463
ER -