3W98

Crystal Structure of Human Nucleosome Core Particle lacking H3.1 N-terminal region

Summary for 3W98

• Entry DOI: 10.2210/pdb3w98/pdb
• Related: 3AFA 3W96 3W97 3W99
• Descriptor: Histone H3.1, Histone H4, Histone H2A type 1-B/E, ... (6 entities in total)
• Functional Keywords: protein-dna complex, histone-fold, nucleosome, structural protein-dna complex, structural protein/dna
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P68431 P62805 P04908 P06899
• Total number of polymer chains: 10
• Total formula weight: 196480.72

Authors

Iwasaki, W.,Miya, Y.,Horikoshi, N.,Osakabe, A.,Tachiwana, H.,Shibata, T.,Kagawa, W.,Kurumizaka, H. (deposition date: 2013-04-01, release date: 2013-08-28, Last modification date: 2023-11-08)

Primary citation

Iwasaki, W.,Miya, Y.,Horikoshi, N.,Osakabe, A.,Taguchi, H.,Tachiwana, H.,Shibata, T.,Kagawa, W.,Kurumizaka, H.
Contribution of histone N-terminal tails to the structure and stability of nucleosomes
FEBS Open Bio, 3:363-369, 2013

PubMed 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.

PubMed: 24251097
DOI: 10.1016/j.fob.2013.08.007

Experimental method

X-RAY DIFFRACTION (3.42 Å)