8CMP

DNA-binding bacterial histone protein HBB from Bdellovibrio bacteriovorus

8CMP の概要

• エントリーDOI: 10.2210/pdb8cmp/pdb
• 分子名称: CBFD_NFYB_HMF domain-containing protein (2 entities in total)
• 機能のキーワード: bacterial histone, dna binding protein
• 由来する生物種: Bdellovibrio bacteriovorus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7189.50

構造登録者

Hu, Y.,Joiner, J.D.,Albrecht, R.,Hartmann, M.D. (登録日: 2023-02-20, 公開日: 2024-03-06, 最終更新日: 2024-10-09)

主引用文献

Hu, Y.,Schwab, S.,Deiss, S.,Escudeiro, P.,van Heesch, T.,Joiner, J.D.,Vreede, J.,Hartmann, M.D.,Lupas, A.N.,Alvarez, B.H.,Alva, V.,Dame, R.T.
Bacterial histone HBb from Bdellovibrio bacteriovorus compacts DNA by bending.
Nucleic Acids Res., 52:8193-8204, 2024

PubMed Abstract: Histones are essential for genome compaction and transcription regulation in eukaryotes, where they assemble into octamers to form the nucleosome core. In contrast, archaeal histones assemble into dimers that form hypernucleosomes upon DNA binding. Although histone homologs have been identified in bacteria recently, their DNA-binding characteristics remain largely unexplored. Our study reveals that the bacterial histone HBb (Bd0055) is indispensable for the survival of Bdellovibrio bacteriovorus, suggesting critical roles in DNA organization and gene regulation. By determining crystal structures of free and DNA-bound HBb, we unveil its distinctive dimeric assembly, diverging from those of eukaryotic and archaeal histones, while also elucidating how it binds and bends DNA through interaction interfaces reminiscent of eukaryotic and archaeal histones. Building on this, by employing various biophysical and biochemical approaches, we further substantiated the ability of HBb to bind and compact DNA by bending in a sequence-independent manner. Finally, using DNA affinity purification and sequencing, we reveal that HBb binds along the entire genomic DNA of B. bacteriovorus without sequence specificity. These distinct DNA-binding properties of bacterial histones, showcasing remarkable similarities yet significant differences from their archaeal and eukaryotic counterparts, highlight the diverse roles histones play in DNA organization across all domains of life.

PubMed: 38864377
DOI: 10.1093/nar/gkae485

実験手法

X-RAY DIFFRACTION (1.06 Å)