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The N-terminal and C-terminal halves of histone H2A.Z independently function in nucleosome positioning and stability.
Genes to Cells ( IF 1.3 ) Pub Date : 2020-06-05 , DOI: 10.1111/gtc.12791
Shoko Sato 1 , Naoki Tanaka 2 , Yasuhiro Arimura 1, 3 , Tomoya Kujirai 1 , Hitoshi Kurumizaka 1, 2
Affiliation  

Nucleosome positioning and stability affect gene regulation in eukaryotic chromatin. Histone H2A.Z is an evolutionally conserved histone variant that forms mobile and unstable nucleosomes in vivo and in vitro. In the present study, we reconstituted nucleosomes containing human H2A.Z.1 mutants, in which the N‐terminal or C‐terminal half of H2A.Z.1 was replaced by the corresponding canonical H2A region. We found that the N‐terminal portion of H2A.Z.1 is involved in flexible nucleosome positioning, whereas the C‐terminal portion leads to weak H2A.Z.1‐H2B association in the nucleosome. These results indicate that the N‐terminal and C‐terminal portions are independently responsible for the H2A.Z.1 nucleosome characteristics.

中文翻译:

组蛋白H2A.Z的N末端和C末端一半在核小体定位和稳定性中独立起作用。

核小体的定位和稳定性影响真核染色质的基因调控。组蛋白H2A.Z是一种进化保守的组蛋白变体,可在体内和体外形成可移动和不稳定的核小体。在本研究中,我们重建了包含人H2A.Z.1突变体的核小体,其中H2A.Z.1的N端或C端一半被相应的规范H2A区取代。我们发现H2A.Z.1的N端部分参与了灵活的核小体定位,而C末端部分导致了H2A.Z.1-H2B在核小体中的缔合较弱。这些结果表明,N末端和C末端部分独立负责H2A.Z.1核小体特征。
更新日期:2020-08-11
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