7WLR

Cryo-EM structure of the nucleosome containing Komagataella pastoris histones

7WLR の概要

• エントリーDOI: 10.2210/pdb7wlr/pdb
• EMDBエントリー: 32591
• 分子名称: Histone H3, Histone H4, Histone H2A, ... (6 entities in total)
• 機能のキーワード: chromatin, nucleosome, komagataella pastoris, histone h2a, histone h2b, histone h3, histone h4, dna, epigenetic, gene regulation, cryo-em, gene regulation-dna complex, gene regulation/dna
• 由来する生物種: Komagataella pastoris; 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 178435.27

構造登録者

Fukushima, Y.,Hatazawa, S.,Hirai, S.,Kujirai, T.,Takizawa, Y.,Kurumizaka, H. (登録日: 2022-01-13, 公開日: 2022-07-13, 最終更新日: 2024-06-26)

主引用文献

Fukushima, Y.,Hatazawa, S.,Hirai, S.,Kujirai, T.,Ehara, H.,Sekine, S.I.,Takizawa, Y.,Kurumizaka, H.
Structural and biochemical analyses of the nucleosome containing Komagataella pastoris histones.
J.Biochem., 172:79-88, 2022

PubMed Abstract: Komagataella pastoris is a methylotrophic yeast that is commonly used as a host cell for protein production. In the present study, we reconstituted the nucleosome with K. pastoris histones and determined the structure of the nucleosome core particle by cryogenic electron microscopy. In the K. pastoris nucleosome, the histones form an octamer and the DNA is left-handedly wrapped around it. Micrococcal nuclease assays revealed that the DNA ends of the K. pastoris nucleosome are somewhat more accessible, as compared with those of the human nucleosome. In vitro transcription assays demonstrated that the K. pastoris nucleosome is transcribed by the K. pastoris RNA polymerase II (RNAPII) more efficiently than the human nucleosome, while the RNAPII pausing positions of the K. pastoris nucleosome are the same as those of the human nucleosome. These results suggested that the DNA end flexibility may enhance the transcription efficiency in the nucleosome but minimally affect the nucleosomal pausing positions of RNAPII.

PubMed: 35485963
DOI: 10.1093/jb/mvac043

実験手法

ELECTRON MICROSCOPY (3.54 Å)