3X1T

Crystal structure of nucleosome core particle consisting of mouse testis specific histone variants H2aa and H2ba

Summary for 3X1T

• Entry DOI: 10.2210/pdb3x1t/pdb
• Related: 3X1S 3X1U 3X1V
• Descriptor: DNA (146-MER), Histone H3.1, Histone H4, ... (8 entities in total)
• Functional Keywords: histone variants of h2a and h2b, reprogramming, chromatin, structural protein-dna complex, structural protein/dna
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P68431 P62805 Q8CGP4 P70696
• Total number of polymer chains: 10
• Total formula weight: 200915.74

Authors

Sivaraman, P.,Kumarevel, T.S. (deposition date: 2014-11-27, release date: 2015-09-23, Last modification date: 2023-11-08)

Primary citation

Padavattan, S.,Shinagawa, T.,Hasegawa, K.,Kumasaka, T.,Ishii, S.,Kumarevel, T.
Structural and functional analyses of nucleosome complexes with mouse histone variants TH2a and TH2b, involved in reprogramming
Biochem.Biophys.Res.Commun., 464:929-935, 2015

PubMed Abstract: Histone variants TH2a and TH2b are highly expressed in testes, oocytes and zygotes. Our recent analysis suggested that these histone variants enhance the induced generation of pluripotent stem cells (iPSCs) when co-expressed along with four transcription factors, Oct3/4, Sox2, Klf4 and c-Myc (OSKM), and are associated with an open chromatin structure [1]. In the present study, we report the crystal structures of nucleosomes (NCPs) with the mouse histone variants, TH2a and TH2b. The structures revealed two significant changes, as compared to the canonical counterparts: fewer histone-DNA contacts and changes in dimer-dimer interactions between TH2a-TH2a' (L1-loop). In vivo studies with domain swapping and point mutants of the variants revealed that the residues in the histone tails and the TH2a-L1 loop are important for reprogramming. Taken together, our work indicates that the NCP variants with structural modifications and flexible tails are most likely important for enhanced reprogramming of functions.

PubMed: 26188507
DOI: 10.1016/j.bbrc.2015.07.070

Experimental method

X-RAY DIFFRACTION (2.808 Å)