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The right place at the right time: chaperoning core histone variants.在正确的时间处于正确的位置:陪伴核心组蛋白变体。
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本文引用的文献

1
Ubinuclein-1 confers histone H3.3-specific-binding by the HIRA histone chaperone complex.泛核仁蛋白-1通过HIRA组蛋白伴侣复合物赋予组蛋白H3.3特异性结合能力。
Nat Commun. 2015 Jul 10;6:7711. doi: 10.1038/ncomms8711.
2
Removal of H2A.Z by INO80 promotes homologous recombination.INO80介导的H2A.Z去除促进同源重组。
EMBO Rep. 2015 Aug;16(8):986-94. doi: 10.15252/embr.201540330. Epub 2015 Jul 3.
3
Histone chaperone Anp32e removes H2A.Z from DNA double-strand breaks and promotes nucleosome reorganization and DNA repair.组蛋白伴侣Anp32e从DNA双链断裂处移除H2A.Z,并促进核小体重组和DNA修复。
Proc Natl Acad Sci U S A. 2015 Jun 16;112(24):7507-12. doi: 10.1073/pnas.1504868112. Epub 2015 Jun 1.
4
The Histone Chaperones FACT and Spt6 Restrict H2A.Z from Intragenic Locations.组蛋白伴侣FACT和Spt6限制H2A.Z在基因内部位置的分布。
Mol Cell. 2015 Jun 18;58(6):1113-23. doi: 10.1016/j.molcel.2015.03.030. Epub 2015 May 7.
5
Chromosomes. CENP-C reshapes and stabilizes CENP-A nucleosomes at the centromere.染色体。着丝粒蛋白C(CENP-C)重塑并稳定着丝粒处的着丝粒蛋白A(CENP-A)核小体。
Science. 2015 May 8;348(6235):699-703. doi: 10.1126/science.1259308.
6
Structural transitions of centromeric chromatin regulate the cell cycle-dependent recruitment of CENP-N.着丝粒染色质的结构转变调控着细胞周期依赖性的CENP-N募集。
Genes Dev. 2015 May 15;29(10):1058-73. doi: 10.1101/gad.259432.115. Epub 2015 May 5.
7
HJURP involvement in de novo CenH3(CENP-A) and CENP-C recruitment.HJURP参与新生CenH3(CENP-A)和CENP-C的招募。
Cell Rep. 2015 Apr 7;11(1):22-32. doi: 10.1016/j.celrep.2015.03.013. Epub 2015 Apr 2.
8
CENP-A K124 Ubiquitylation Is Required for CENP-A Deposition at the Centromere.着丝粒抗原 A 赖氨酸 124 泛素化对于着丝粒抗原 A 在着丝粒处的沉积是必需的。
Dev Cell. 2015 Mar 9;32(5):589-603. doi: 10.1016/j.devcel.2015.01.024. Epub 2015 Feb 26.
9
Dynamic phosphorylation of CENP-A at Ser68 orchestrates its cell-cycle-dependent deposition at centromeres.动态磷酸化的 CENP-A 在丝氨酸 68 处协调其在着丝粒处的细胞周期依赖性沉积。
Dev Cell. 2015 Jan 12;32(1):68-81. doi: 10.1016/j.devcel.2014.11.030. Epub 2014 Dec 31.
10
MacroH2A1.1 and PARP-1 cooperate to regulate transcription by promoting CBP-mediated H2B acetylation.MacroH2A1.1与聚(ADP-核糖)聚合酶-1通过促进CBP介导的H2B乙酰化协同调节转录。
Nat Struct Mol Biol. 2014 Nov;21(11):981-9. doi: 10.1038/nsmb.2903. Epub 2014 Oct 12.

在正确的时间处于正确的位置:陪伴核心组蛋白变体。

The right place at the right time: chaperoning core histone variants.

作者信息

Mattiroli Francesca, D'Arcy Sheena, Luger Karolin

机构信息

Department of Molecular and Radiobiological Sciences, Howard Hughes Medical Institute, Colorado State University, Fort Collins, CO, USA

Department of Molecular and Radiobiological Sciences, Howard Hughes Medical Institute, Colorado State University, Fort Collins, CO, USA.

出版信息

EMBO Rep. 2015 Nov;16(11):1454-66. doi: 10.15252/embr.201540840. Epub 2015 Oct 12.

DOI:10.15252/embr.201540840
PMID:26459557
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4641499/
Abstract

Histone proteins dynamically regulate chromatin structure and epigenetic signaling to maintain cell homeostasis. These processes require controlled spatial and temporal deposition and eviction of histones by their dedicated chaperones. With the evolution of histone variants, a network of functionally specific histone chaperones has emerged. Molecular details of the determinants of chaperone specificity for different histone variants are only slowly being resolved. A complete understanding of these processes is essential to shed light on the genuine biological roles of histone variants, their chaperones, and their impact on chromatin dynamics.

摘要

组蛋白动态调节染色质结构和表观遗传信号,以维持细胞内稳态。这些过程需要其特定伴侣蛋白对组蛋白进行可控的时空沉积和移除。随着组蛋白变体的进化,一个功能特异的组蛋白伴侣蛋白网络已经出现。不同组蛋白变体伴侣蛋白特异性决定因素的分子细节正在缓慢得到解析。全面了解这些过程对于阐明组蛋白变体、其伴侣蛋白的真正生物学作用及其对染色质动力学的影响至关重要。