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富含精氨酸的组蛋白核心对140个碱基对长度的DNA进行折叠。

Folding of 140-base pair length DNA by a core of arginine-rich histones.

作者信息

Bina-Stein M

出版信息

J Biol Chem. 1978 Jul 25;253(14):5213-9.

PMID:670187
Abstract

The nucleoprotein complex obtained by reconstitution of arginine-rich histones with 140-base pair length DNA has properties considerably closer to native core particles than the complex obtained with lysine-rich histones. A tetramer of arginine-rich histones folds 140-base pair length DNA into a particle (R body) with identical projections, on high resolution electron micrographs, as native core particles. The R body is more spherical in shape than the native nucleosome core particle. Both arginine- and lysine-rich histones contribute to the altered thermal stability and circular dichroism spectra of the core particle DNA.

摘要

通过将富含精氨酸的组蛋白与140个碱基对长度的DNA重构获得的核蛋白复合物,其性质比用富含赖氨酸的组蛋白获得的复合物更接近天然核心颗粒。在高分辨率电子显微镜下,富含精氨酸的组蛋白四聚体将140个碱基对长度的DNA折叠成具有与天然核心颗粒相同突起的颗粒(R体)。R体的形状比天然核小体核心颗粒更呈球形。富含精氨酸和赖氨酸的组蛋白都导致核心颗粒DNA的热稳定性和圆二色光谱发生改变。

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