Real-time observation of nucleoplasmin-mediated DNA decondensation and condensation reveals its specific functions as a chaperone
文献类型: 外文期刊
第一作者: Huo, Xin-Mei
作者: Huo, Xin-Mei;Meng, Li-feng;Li, Jian-Ke;Jiang, Tao;Sun, Fang-Zhen;Li, Ming;Sun, Bo
作者机构:
关键词: Nucleoplasmin; Magnetic tweezers; DNA condensation; Decondensation; Chromatin remodeling
期刊名称:BIOCHIMICA ET BIOPHYSICA ACTA-GENE REGULATORY MECHANISMS ( 影响因子:4.49; 五年影响因子:5.318 )
ISSN: 1874-9399
年卷期: 2018 年 1861 卷 8 期
页码:
收录情况: SCI
摘要: Fertilization requires decondensation of promatine-condensed sperm chromatin, a dynamic process serving as an attractive system for the study of chromatin reprogramming. Nucleoplasmin is a key factor in regulating nucleosome assembly as a chaperone during fertilization process. However, knowledge on nucleoplasmin in chromatin formation remains elusive. Herein, magnetic tweezers (MT) and a chromatin assembly system were used to study the nucleoplasmin-mediated DNA decondensation/condensation at the single-molecular level in vitro. We found that protamine induces DNA condensation in a stepwise manner. Once DNA was condensed, nucleoplasmin, polyglutamic acid, and RNA could remove protamine from the DNA at different rates. The affinity binding of the different polyanions with protamine suggests chaperone-mediated chromatin decondensation activity occurs through protein protein interactions. After decondensation, both RNA and polyglutamic acid prevented the transfer of histones onto the naked DNA. In contrast, nucleoplasmin is able to assist the histone transfer process, even though it carries the same negative charge as RNA and polyglutamic acid. These observations imply that the chaperone effects of nucleoplasmin during the decondensation/condensation process may be driven by specific spatial configuration of its acidic pentamer structure, rather than by electrostatic interaction. Our findings offer a novel molecular understanding of nucleoplasmin in sperm chromatin decondensation and subsequent developmental chromatin reprogramming at individual molecular level.
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