Send to

Choose Destination
FEBS Open Bio. 2013 Aug 22;3:363-9. doi: 10.1016/j.fob.2013.08.007. eCollection 2013.

Contribution of histone N-terminal tails to the structure and stability of nucleosomes.

Author information

Laboratory of Structural Biology, Graduate School of Advanced Science and Engineering, Waseda University, 2-2 Wakamatsu-cho, Shinjuku-ku, Tokyo 162-8480, Japan ; RIKEN, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan.


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.


Chromatin; Crystal structure; Histone tail; Nucleosome; PDB, Protein Data Bank; RMSD, root mean square deviation; SHL, superhelical location; Thermal stability assay; tlH2A, human histone H2A lacking N-terminal tail; tlH2B, human histone H2B lacking N-terminal tail; tlH3, human histone H3 lacking N-terminal tail; tlH4, human histone H4 lacking N-terminal tail; wt, wild-type

Supplemental Content

Full text links

Icon for Wiley Icon for PubMed Central
Loading ...
Support Center