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首页> 外文期刊>Molecular and Cellular Biology >Histone Deacetylases and Phosphorylated Polymerase II C-Terminal Domain Recruit Spt6 for Cotranscriptional Histone Reassembly
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Histone Deacetylases and Phosphorylated Polymerase II C-Terminal Domain Recruit Spt6 for Cotranscriptional Histone Reassembly

机译：组蛋白去乙酰化酶和磷酸化聚合酶II C末端域招募Spt6用于共转录组蛋白重组。

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摘要

Spt6 is a multifunctional histone chaperone involved in the maintenance of chromatin structure during elongation by RNA polymerase II (Pol II). Spt6 has a tandem SH2 (tSH2) domain within its C terminus that recognizes Pol II C-terminal domain (CTD) peptides phosphorylated on Ser2, Ser5, or Try1 in vitro. Deleting the tSH2 domain, however, only has a partial effect on Spt6 occupancy in vivo, suggesting that more complex mechanisms are involved in the Spt6 recruitment. Our results show that the Ser2 kinases Bur1 and Ctk1, but not the Ser5 kinase Kin28, cooperate in recruiting Spt6, genome-wide. Interestingly, the Ser2 kinases promote the association of Spt6 in early transcribed regions and not toward the 3′ ends of genes, where phosphorylated Ser2 reaches its maximum level. In addition, our results uncover an unexpected role for histone deacetylases (Rpd3 and Hos2) in promoting Spt6 interaction with elongating Pol II. Finally, our data suggest that phosphorylation of the Pol II CTD on Tyr1 promotes the association of Spt6 with the 3′ ends of transcribed genes, independently of Ser2 phosphorylation. Collectively, our results show that a complex network of interactions, involving the Spt6 tSH2 domain, CTD phosphorylation, and histone deacetylases, coordinate the recruitment of Spt6 to transcribed genes in vivo.
机译：Spt6是一种多功能的组蛋白分子伴侣，参与RNA聚合酶II（Pol II）延伸过程中染色质结构的维持。 Spt6在其C末端具有一个串联SH2（tSH2）结构域，该结构域可以识别在Ser2，Ser5或Try1上磷酸化的Pol II C末端结构域（CTD）肽。然而，删除tSH2结构域仅对体内Spt6的占有率产生部分影响，表明Spt6募集涉及更复杂的机制。我们的结果表明，Ser2激酶Bur1和Ctk1，而不是Ser5激酶Kin28，在招募全基因组的Spt6方面起着协同作用。有趣的是，Ser2激酶促进Spt6在早期转录区域中的缔合，而不是向磷酸化Ser2达到其最高水平的基因的3'端促进。此外，我们的结果揭示了组蛋白脱乙酰基酶（Rpd3和Hos2）在促进Spt6与延长Pol II相互作用中的意外作用。最后，我们的数据表明，Tyr1上Pol II CTD的磷酸化促进了Spt6与转录基因3'末端的缔合，而与Ser2磷酸化无关。总体而言，我们的研究结果表明，一个复杂的相互作用网络涉及Spt6 tSH2域，CTD磷酸化和组蛋白脱乙酰基酶，可以协调Spt6募集到转录的体内基因。

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