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Bala Bharathi Burugula Célia Jeronimo Rakesh Pathak Jeffery W. Jones Fran?ois Robert Chhabi K. Govind 《Molecular and cellular biology》2014,34(22):4115-4129
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. 相似文献
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The Spt4p subunit of yeast DSIF stimulates association of the Paf1 complex with elongating RNA polymerase II
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The Paf1 complex (Paf1C) interacts with RNA polymerase II (Pol II) and promotes histone methylation of transcribed coding sequences, but the mechanism of Paf1C recruitment is unknown. We show that Paf1C is not recruited directly by the activator Gcn4p but is dependent on preinitiation complex assembly and Ser5 carboxy-terminal domain phosphorylation for optimal association with ARG1 coding sequences. Importantly, Spt4p is required for Paf1C occupancy at ARG1 (and other genes) and for Paf1C association with Ser5-phosphorylated Pol II in cell extracts, whereas Spt4p-Pol II association is independent of Paf1C. Since spt4Delta does not reduce levels of Pol II at ARG1, Ser5 phosphorylation, or Paf1C expression, it appears that Spt4p (or its partner in DSIF, Spt5p) provides a platform on Pol II for recruiting Paf1C following Ser5 phosphorylation and promoter clearance. spt4Delta reduces trimethylation of Lys4 on histone H3, demonstrating a new role for yeast DSIF in promoting a Paf1C-dependent function in elongation. 相似文献
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Sandip De David M Edwards Vibha Dwivedi Jianming Wang Wazeer Varsally Hannah
L Dixon Anand
K Singh Precious O Owuamalam Matthew T Wright Reece P Summers Md Nazmul Hossain Emily
M Price Marcin
W Wojewodzic Francesco Falciani Nikolas J Hodges Marco Saponaro Kayoko Tanaka Claus M Azzalin Peter Baumann Daniel Hebenstreit Saverio Brogna 《Nucleic acids research》2022,50(1):350
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Gwendal Le Martelot Donatella Canella Laura Symul Eugenia Migliavacca Federica Gilardi Robin Liechti Olivier Martin Keith Harshman Mauro Delorenzi Béatrice Desvergne Winship Herr Bart Deplancke Ueli Schibler Jacques Rougemont Nicolas Guex Nouria Hernandez Felix Naef the CycliX consortium 《PLoS biology》2012,10(11)
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