• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Nucleus >Unveiling novel interactions of histone chaperone Asf1 linked to TREX-2 factors Sus1 and Thp1
【24h】

Unveiling novel interactions of histone chaperone Asf1 linked to TREX-2 factors Sus1 and Thp1

机译：揭示与TREX-2因子Sus1和Thp1相关的组蛋白伴侣Asf1的新型相互作用

获取原文
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Anti-silencing function 1 (Asf1) is a conserved key eukaryotic histone H3/H4 chaperone that participates in a variety of DNA and chromatin-related processes. These include the assembly and disassembly of histones H3 and H4 from chromatin during replication, transcription, and DNA repair. In addition, Asf1 is required for H3K56 acetylation activity dependent on histone acetyltransferase Rtt109. Thus, Asf1 impacts on many aspects of DNA metabolism. To gain insights into the functional links of Asf1 with other cellular machineries, we employed mass spectrometry coupled to tandem affinity purification (TAP) to investigate novel physical interactions of Asf1. Under different TAP-MS analysis conditions, we describe a new repertoire of Asf1 physical interactions and novel Asf1 post-translational modifications as ubiquitination, methylation and acetylation that open up new ways to regulate Asf1 functions. Asf1 co-purifies with several subunits of the TREX-2, SAGA complexes, and with nucleoporins Nup2, Nup60, and Nup57, which are all involved in transcription coupled to mRNA export in eukaryotes. Reciprocally, Thp1 and Sus1 interact with Asf1. Albeit mRNA export and GAL1 transcription are not affected in asf1Δ a strong genetic interaction exists between ASF1 and SUS1 . Notably, supporting a functional link between Asf1 and TREX-2, both Sus1 and Thp1 affect the levels of Asf1-dependent histone H3K56 acetylation and histone H3 and H4 incorporation onto chromatin. Additionally, we provide evidence for a role of Asf1 in histone H2B ubiquitination. This work proposes a functional link between Asf1 and TREX-2 components in histone metabolism at the vicinity of the nuclear pore complex.
机译：抗沉默功能1（Asf1）是保守的关键真核组蛋白H3 / H4分子伴侣，参与各种DNA和染色质相关过程。这些包括在复制，转录和DNA修复过程中从染色质组装和拆卸组蛋白H3和H4。另外，依赖于组蛋白乙酰基转移酶Rtt109的H3K56乙酰化活性需要Asf1。因此，ASF1影响DNA代谢的许多方面。为了深入了解Asf1与其他细胞机械的功能联系，我们使用了质谱联用串联亲和纯化（TAP）来研究Asf1的新型物理相互作用。在不同的TAP-MS分析条件下，我们描述了Asf1物理相互作用的新功能以及新的Asf1翻译后修饰（如泛素化，甲基化和乙酰化），为调节Asf1功能开辟了新途径。 Asf1与TREX-2，SAGA复合物的几个亚基以及核孔蛋白Nup2，Nup60和Nup57共纯化，它们都参与与真核生物中mRNA输出耦合的转录。相反，Thp1和Sus1与Asf1相互作用。尽管在asf1Δ中不影响mRNA的输出和转录，但 ASF1和之间仍存在很强的遗传相互作用。值得注意的是，支持Asf1和TREX-2之间的功能链接，Sus1和Thp1都影响依赖于Asf1的组蛋白H3K56乙酰化水平以及组蛋白H3和H4掺入染色质的水平。另外，我们提供了Asf1在组蛋白H2B泛素化中的作用的证据。这项工作提出了在核孔复合物附近的组蛋白代谢中Asf1和TREX-2组分之间的功能联系。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号