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微小核特异性组蛋白H1是嗜热四膜虫微小核染色体完整性所必需的。

Micronucleus-specific histone H1 is required for micronuclear chromosome integrity in Tetrahymena thermophila.

作者信息

Qiao Juxia, Xu Jing, Bo Tao, Wang Wei

机构信息

Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education, Institute of Biotechnology, Shanxi University, Taiyuan, Shanxi, China.

College of Life Science, Shanxi University, Taiyuan, Shanxi, China.

出版信息

PLoS One. 2017 Nov 2;12(11):e0187475. doi: 10.1371/journal.pone.0187475. eCollection 2017.

Abstract

Histone H1 molecules play a key role in establishing and maintaining higher order chromatin structures. They can bind to linker DNA entering and exiting the nucleosome and regulate transcriptional activity. Tetrahymena thermophila has two histone H1, namely, macronuclear histone H1 and micronuclear histone H1 (Mlh1). Mlh1 is specifically localized at micronuclei during growth and starvation stages. Moreover, Mlh1 is localized around micronuclei and forms a specific structure during the conjugation stage. It co-localizes partially with spindle apparatus during micronuclear meiosis. Analysis of MLH1 knock-out revealed that Mlh1 was required for the micronuclear integrity and development during conjugation stage. Overexpression of Mlh1 led to abnormal conjugation progression. RT-PCR analysis indicated that the expression level of HMGB3 increased in ΔMLH1 strains, while the expression level of MLH1 increased in ΔHMGB3 cells during conjugation. These results indicate that micronuclear integrity and sexual development require normal expression level of Mlh1 and that HmgB3 and Mlh1 may functionally compensate each other in regulating micronuclear structure in T. thermophila.

摘要

组蛋白H1分子在建立和维持高阶染色质结构中起关键作用。它们可以结合进出核小体的连接DNA并调节转录活性。嗜热四膜虫有两种组蛋白H1,即大核组蛋白H1和小核组蛋白H1(Mlh1)。Mlh1在生长和饥饿阶段特异性定位于小核。此外,Mlh1在接合阶段定位于小核周围并形成特定结构。在小核减数分裂期间,它与纺锤体部分共定位。MLH1敲除分析表明,Mlh1是接合阶段小核完整性和发育所必需的。Mlh1的过表达导致接合进程异常。RT-PCR分析表明,在接合过程中,ΔMLH1菌株中HMGB3的表达水平增加,而ΔHMGB3细胞中MLH1的表达水平增加。这些结果表明,小核完整性和有性发育需要Mlh1的正常表达水平,并且HmgB3和Mlh1可能在调节嗜热四膜虫小核结构中发挥功能互补作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a450/5667856/447d1d8fb172/pone.0187475.g001.jpg

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